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Conserved domains on  [gi|1039778538|ref|XP_017177711|]
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liprin-alpha-1 isoform X16 [Mus musculus]

Protein Classification

liprin-alpha( domain architecture ID 13377566)

liprin-alpha belongs to the LAR (leukocyte common antigen-related) family or transmembrane protein-tyrosine phosphatase-interacting proteins and is involved in formation of the presynaptic active zone

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 991-1056 3.82e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188964  Cd Length: 66  Bit Score: 150.70  E-value: 3.82e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039778538  991 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1056
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 874-944 1.32e-42

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188961  Cd Length: 71  Bit Score: 149.64  E-value: 1.32e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039778538  874 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLT 944
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1076-1147 2.84e-42

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188967  Cd Length: 72  Bit Score: 148.62  E-value: 2.84e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039778538 1076 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1147
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 260-512 7.84e-17

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 86.14  E-value: 7.84e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  260 RQARE-QSQMKERLASLSSHA-AELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATS 337
Cdd:COG1196    213 ERYRElKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  338 VHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKL----QQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEE 413
Cdd:COG1196    293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  414 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLsdtvDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 493
Cdd:COG1196    373 ELAEAEEELEELAEELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                          250
                   ....*....|....*....
gi 1039778538  494 HDKDQLVVTIEALKAELEQ 512
Cdd:COG1196    449 EEEAELEEEEEALLELLAE 467
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 54-432 1.07e-12

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 72.78  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   54 LRETQETLALTQGKLHEVGHERDSLQRQLNTAlpQEFAALTKELNvcREQLLEREEEIAELKAERNNTRLLLEHLECLVS 133
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELE 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  134 RHERSLrmtvvkrqaqspagvssevevlKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQk 213
Cdd:TIGR02168  257 ELTAEL----------------------QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN- 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  214 ktltdglLDGNHEQESAPSTNGKRSSDgsLSHEDLA----KVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTA 289
Cdd:TIGR02168  314 -------LERQLEELEAQLEELESKLD--ELAEELAeleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  290 RKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQER 369
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEA 462

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039778538  370 LELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRA 432
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 389-660 5.35e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 5.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  389 EVEAELAQRVAALSKAEERhgniEERLRQMeaqLEEKNQELQR-ARQREKMNEehnkrlsdtVDKLLSESNE-RLQLHLK 466
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEEN----IERLDLI---IDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLK 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  467 ERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRphlgsVPDFRFSVADGHVD--- 543
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE-----QLRVKEKIGELEAEias 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  544 AYSTSAVLRRPQK---GRLAALRDEPSKVQ-TLNEQDWERAQQASVLANVAQAFESDvdvsdgEDDRDTLLSSVDLLSPS 619
Cdd:TIGR02169  306 LERSIAEKERELEdaeERLAKLEAEIDKLLaEIEELEREIEEERKRRDKLTEEYAEL------KEELEDLRAELEEVDKE 379

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1039778538  620 GQA------DAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIE 660
Cdd:TIGR02169  380 FAEtrdelkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 991-1056 3.82e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188964  Cd Length: 66  Bit Score: 150.70  E-value: 3.82e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039778538  991 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1056
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 874-944 1.32e-42

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188961  Cd Length: 71  Bit Score: 149.64  E-value: 1.32e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039778538  874 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLT 944
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1076-1147 2.84e-42

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188967  Cd Length: 72  Bit Score: 148.62  E-value: 2.84e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039778538 1076 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1147
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 260-512 7.84e-17

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 86.14  E-value: 7.84e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  260 RQARE-QSQMKERLASLSSHA-AELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATS 337
Cdd:COG1196    213 ERYRElKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  338 VHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKL----QQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEE 413
Cdd:COG1196    293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  414 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLsdtvDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 493
Cdd:COG1196    373 ELAEAEEELEELAEELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                          250
                   ....*....|....*....
gi 1039778538  494 HDKDQLVVTIEALKAELEQ 512
Cdd:COG1196    449 EEEAELEEEEEALLELLAE 467
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 246-516 2.68e-15

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 81.26  E-value: 2.68e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  246 EDLAKVLELQ-EVIDRQAREQSQMKE--------RLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKED 316
Cdd:TIGR02168  192 EDILNELERQlKSLERQAEKAERYKElkaelrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  317 MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ 396
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  397 RVAALSKAEERHG----NIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdKLLSESNERLQLHLKERMAAL 472
Cdd:TIGR02168  352 ELESLEAELEELEaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEELLKKL 430

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1039778538  473 E--DKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:TIGR02168  431 EeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 990-1054 4.99e-13

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 64.98  E-value: 4.99e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039778538  990 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1054
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 54-432 1.07e-12

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 72.78  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   54 LRETQETLALTQGKLHEVGHERDSLQRQLNTAlpQEFAALTKELNvcREQLLEREEEIAELKAERNNTRLLLEHLECLVS 133
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELE 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  134 RHERSLrmtvvkrqaqspagvssevevlKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQk 213
Cdd:TIGR02168  257 ELTAEL----------------------QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN- 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  214 ktltdglLDGNHEQESAPSTNGKRSSDgsLSHEDLA----KVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTA 289
Cdd:TIGR02168  314 -------LERQLEELEAQLEELESKLD--ELAEELAeleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  290 RKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQER 369
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEA 462

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039778538  370 LELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRA 432
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
158-514 1.90e-11

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 68.53  E-value: 1.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  158 VEVLKALKSLFEHHkaldEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKR 237
Cdd:PRK02224   233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  238 SSDGSLSHEDLAKVL-ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKED 316
Cdd:PRK02224   309 AEAVEARREELEDRDeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  317 MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQklqqtLRKAETLPEVEAEL-- 394
Cdd:PRK02224   389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVeg 463

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  395 AQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLS--DTVDKLLSESNERLQ------LHLK 466
Cdd:PRK02224   464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEekreraEELR 543

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1039778538  467 ERMAALEDKNSLLREVenAKKQLEETQhDKDQLVVTIEALKAELEQMR 514
Cdd:PRK02224   544 ERAAELEAEAEEKREA--AAEAEEEAE-EAREEVAELNSKLAELKERI 588
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 205-511 7.51e-11

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 66.68  E-value: 7.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  205 ILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVL---------------ELQEVIDRQAREQSQMK 269
Cdd:pfam15921  132 IRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMlshegvlqeirsilvDFEEASGKKIYEHDSMS 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  270 E-RLASLSSHAAELEEDLDTARKDLI--------KSEEMNTKLQREVREAMAQKEDMEER--------ITTLEKRYLAAQ 332
Cdd:pfam15921  212 TmHFRSLGSAISKILRELDTEISYLKgrifpvedQLEALKSESQNKIELLLQQHQDRIEQliseheveITGLTEKASSAR 291

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  333 REATSVHDLNDKLENEIANKDSMHRqtedknRQLQErLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAE------- 405
Cdd:pfam15921  292 SQANSIQSQLEIIQEQARNQNSMYM------RQLSD-LESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEltearte 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  406 -----ERHGNIEERLRQMEAQLEEKNQELQrarqrekMNEEHNKRLSD-------TVDKLLSESNER------------- 460
Cdd:pfam15921  365 rdqfsQESGNLDDQLQKLLADLHKREKELS-------LEKEQNKRLWDrdtgnsiTIDHLRRELDDRnmevqrleallka 437

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039778538  461 ----LQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELE 511
Cdd:pfam15921  438 mkseCQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
44-468 2.75e-08

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.24  E-value: 2.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:COG4717     87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRELEEELE 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  123 LLLEHLECLVSRHERSLRmtvvkrqaqspagvSSEVEVLKALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGAT 199
Cdd:COG4717    167 ELEAELAELQEELEELLE--------------QLSLATEEELQDLAEELEELQQRLaelEEELEEAQEELEELEEELEQL 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  200 HKELMILKEQNNQKKTLTDGLLDGnheqeSAPSTNGKRSSDGSLSHEDLAKVLELQEVI-------DRQAREQSQMKERL 272
Cdd:COG4717    233 ENELEAAALEERLKEARLLLLIAA-----ALLALLGLGGSLLSLILTIAGVLFLVLGLLallflllAREKASLGKEAEEL 307

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  273 ASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANK 352
Cdd:COG4717    308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL 387

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  353 DSMHRQTEDKnRQLQERLELAEQKLQQ------TLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE--E 424
Cdd:COG4717    388 RAALEQAEEY-QELKEELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlE 466

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1039778538  425 KNQELQRARQREKMNEEHNKRLSD--TVDKLLSESNERLQLHLKER 468
Cdd:COG4717    467 EDGELAELLQELEELKAELRELAEewAALKLALELLEEAREEYREE 512
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1077-1147 1.36e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.60  E-value: 1.36e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039778538  1077 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDfsalaLLLQIPTQNTQARAVLEREFNNLL 1147
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 874-940 3.35e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.45  E-value: 3.35e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039778538   874 FAQWDGPTVVVWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEI 940
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 999-1054 3.48e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.45  E-value: 3.48e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039778538   999 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1054
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 36-438 9.92e-06

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 49.30  E-value: 9.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   36 FEQLMVSMLEERDRL--LDTLRE---------TQETLALTQGKLHEVGHERD-SLQRQLNTALPQEFAALTKELNVCREQ 103
Cdd:pfam19220    5 NELLRVRLGEMADRLedLRSLKAdfsqliepiEAILRELPQAKSRLLELEALlAQERAAYGKLRRELAGLTRRLSAAEGE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  104 LLEREEEIAELKAERNNTRLLLEHLECLVSrhERSLRMTVVKRQAqspagvSSEVEVLKALKslfEHHKALdekvRERLR 183
Cdd:pfam19220   85 LEELVARLAKLEAALREAEAAKEELRIELR--DKTAQAEALERQL------AAETEQNRALE---EENKAL----REEAQ 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  184 VALERCSLLEEELGATHKELMILKEQNNQKKTLTDglldgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEV--IDRQ 261
Cdd:pfam19220  150 AAEKALQRAEGELATARERLALLEQENRRLQALSE-------EQAAELAELTRRLAELETQLDATRARLRALEGqlAAEQ 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  262 AREQSQMKERLASLSSHAAE---LEEDLDTARKDLIKSEEMNTklqrevrEAMAQKEDMEERITTLEKRYLAAQREATSV 338
Cdd:pfam19220  223 AERERAEAQLEEAVEAHRAErasLRMKLEALTARAAATEQLLA-------EARNQLRDRDEAIRAAERRLKEASIERDTL 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  339 HDLNDKLENEIANKDSMHRQTEDKNRQLQERLElaeqklqqTLRKAetlpeveaeLAQRVAALSKAEERHGNIEERLRQM 418
Cdd:pfam19220  296 ERRLAGLEADLERRTQQFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIASLSDRIAEL 358

                          410       420
                   ....*....|....*....|....*..
gi 1039778538  419 E-------AQLEEKNQELQRARQREKM 438
Cdd:pfam19220  359 TkrfeverAALEQANRRLKEELQRERA 385
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1077-1147 4.40e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 42.64  E-value: 4.40e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039778538 1077 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFsalalLLQIPTQNTQARAVLEREFNNLL 1147
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLED-----LKRLGITSVGHRRKILKKIQELK 66
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 323-444 1.42e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153364 [Multi-domain]  Cd Length: 258  Bit Score: 41.96  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  323 TLEKRYLAAQREATSVHDLNDKLENEIAN----------KDSMHRQTE---DKNRQLQERLELAEQKLQQTLRKAETLPE 389
Cdd:cd07680     61 SLERAWGAIMTEADKVSELHQEVKNNLLNedlekvknwqKDAYHKQIMggfKETKEAEDGFRKAQKPWAKKMKELEAAKK 140

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039778538  390 V------EAELAQRVAALSKAEErhGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNK 444
Cdd:cd07680    141 AyhlackEEKLAMTREANSKAEQ--SVTPEQQKKLQDKVDKCKQDVQKTQEKyEKVLDDVGK 200
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 876-938 1.60e-03

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 38.02  E-value: 1.60e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039778538  876 QWDGPTVVVWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQ 938
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQ 61
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 389-660 5.35e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 5.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  389 EVEAELAQRVAALSKAEERhgniEERLRQMeaqLEEKNQELQR-ARQREKMNEehnkrlsdtVDKLLSESNE-RLQLHLK 466
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEEN----IERLDLI---IDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLK 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  467 ERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRphlgsVPDFRFSVADGHVD--- 543
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE-----QLRVKEKIGELEAEias 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  544 AYSTSAVLRRPQK---GRLAALRDEPSKVQ-TLNEQDWERAQQASVLANVAQAFESDvdvsdgEDDRDTLLSSVDLLSPS 619
Cdd:TIGR02169  306 LERSIAEKERELEdaeERLAKLEAEIDKLLaEIEELEREIEEERKRRDKLTEEYAEL------KEELEDLRAELEEVDKE 379

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1039778538  620 GQA------DAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIE 660
Cdd:TIGR02169  380 FAEtrdelkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 991-1056 3.82e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188964  Cd Length: 66  Bit Score: 150.70  E-value: 3.82e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039778538  991 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1056
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 874-944 1.32e-42

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188961  Cd Length: 71  Bit Score: 149.64  E-value: 1.32e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039778538  874 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLT 944
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1076-1147 2.84e-42

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188967  Cd Length: 72  Bit Score: 148.62  E-value: 2.84e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039778538 1076 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1147
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 995-1054 4.09e-29

SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188894  Cd Length: 60  Bit Score: 110.70  E-value: 4.09e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  995 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1054
Cdd:cd09495      1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 881-939 1.35e-26

SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188893  Cd Length: 58  Bit Score: 103.46  E-value: 1.35e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039778538  881 TVVVWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 939
Cdd:cd09494      1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 1084-1145 2.48e-24

SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188895  Cd Length: 62  Bit Score: 97.23  E-value: 2.48e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039778538 1084 RVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNN 1145
Cdd:cd09496      1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 1076-1147 7.26e-22

SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188969  Cd Length: 72  Bit Score: 90.58  E-value: 7.26e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039778538 1076 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1147
Cdd:cd09570      1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 260-512 7.84e-17

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 86.14  E-value: 7.84e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  260 RQARE-QSQMKERLASLSSHA-AELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATS 337
Cdd:COG1196    213 ERYRElKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  338 VHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKL----QQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEE 413
Cdd:COG1196    293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  414 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLsdtvDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 493
Cdd:COG1196    373 ELAEAEEELEELAEELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                          250
                   ....*....|....*....
gi 1039778538  494 HDKDQLVVTIEALKAELEQ 512
Cdd:COG1196    449 EEEAELEEEEEALLELLAE 467
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 248-517 8.90e-17

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 86.14  E-value: 8.90e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  248 LAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKR 327
Cdd:COG1196    231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  328 YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQT----LRKAETLPEVEAELAQRVAALSK 403
Cdd:COG1196    311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeealLEAEAELAEAEEELEELAEELLE 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  404 AEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL---LSESNERLQLHLKERMAALEDKNSLLR 480
Cdd:COG1196    391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEeeaLEEAAEEEAELEEEEEALLELLAELLE 470

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1039778538  481 EVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRG 517
Cdd:COG1196    471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 875-939 2.09e-16

SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188963  Cd Length: 70  Bit Score: 74.80  E-value: 2.09e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039778538  875 AQWDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 939
Cdd:cd09564      2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 1076-1147 1.13e-15

SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188968  Cd Length: 72  Bit Score: 72.87  E-value: 1.13e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039778538 1076 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1147
Cdd:cd09569      1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 246-516 2.68e-15

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 81.26  E-value: 2.68e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  246 EDLAKVLELQ-EVIDRQAREQSQMKE--------RLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKED 316
Cdd:TIGR02168  192 EDILNELERQlKSLERQAEKAERYKElkaelrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  317 MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ 396
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  397 RVAALSKAEERHG----NIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdKLLSESNERLQLHLKERMAAL 472
Cdd:TIGR02168  352 ELESLEAELEELEaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEELLKKL 430

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1039778538  473 E--DKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:TIGR02168  431 EeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 990-1054 2.77e-15

SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188966  Cd Length: 65  Bit Score: 71.29  E-value: 2.77e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039778538  990 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1054
Cdd:cd09567      1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 990-1054 2.81e-15

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188965  Cd Length: 63  Bit Score: 71.19  E-value: 2.81e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039778538  990 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1054
Cdd:cd09566      1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 192-516 2.24e-14

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 78.57  E-value: 2.24e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  192 LEEELGATHKELMILKEQNNQKKTLTDGLLDgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIdrqAREQSQMKER 271
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDELSQ---ELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL---EEDLSSLEQE 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  272 LASLSSHAAELEEDLDTARKDLIKSEEMNTKLQRE-----VREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLE 346
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  347 NEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQL---E 423
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKE----------ELEEELEELEAALRDLESRLGDLKKERDELEAQLrelE 902

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  424 EKNQELQRARQREKMN-----------EEHNKRLSDTVDKLLSESNERLQLH-LKERMAALEDKNSLLREVEN-AKKQLE 490
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRlselkaklealEEELSEIEDPKGEDEEIPEEELSLEdVQAELQRVEEEIRALEPVNMlAIQEYE 982

                          330       340
                   ....*....|....*....|....*.
gi 1039778538  491 ETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:TIGR02169  983 EVLKRLDELKEKRAKLEEERKAILER 1008
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 253-516 4.36e-14

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 77.40  E-value: 4.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQ 332
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  333 REATSVHDLNDKLENEIAnkdsmhrQTEDKNRQLQERLELAEQKLQQTlrkAETLPEVEAELAQRVAALSKAEERHGNIE 412
Cdd:TIGR02168  761 AEIEELEERLEEAEEELA-------EAEAEIEELEAQIEQLKEELKAL---REALDELRAELTLLNEEAANLRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  413 ERLRQMEAQLEEKNQELQRAR-QREKMNEEHNKrlsdtVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEE 491
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSeDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905

                          250       260
                   ....*....|....*....|....*
gi 1039778538  492 TQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLELR 930
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 245-474 1.20e-13

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 75.74  E-value: 1.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  245 HEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTL 324
Cdd:COG1196    284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  325 EKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKA 404
Cdd:COG1196    364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  405 EErhgniEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLsdtvDKLLSESNERLQLHLKERMAALED 474
Cdd:COG1196    444 LE-----EAAEEEAELEEEEEALLELLAELLEEAALLEAALA----ELLEELAEAAARLLLLLEAEADYE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 192-464 4.72e-13

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 73.94  E-value: 4.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  192 LEEELGATHKELMI--LKEQNNQKKTLTDGLLDGNHEQESApsTNGKRSSDGSLS------HEDLAKVLELQEVIDRQAR 263
Cdd:TIGR02168  218 LKAELRELELALLVlrLEELREELEELQEELKEAEEELEEL--TAELQELEEKLEelrlevSELEEEIEELQKELYALAN 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  264 EQSQM-------KERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITT-------LEKRYL 329
Cdd:TIGR02168  296 EISRLeqqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEleaeleeLESRLE 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  330 AAQREATSVHDLNDKLENEIA--------NKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK-AETLPEVEAELAQRVAA 400
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIAslnneierLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEE 455

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039778538  401 LSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLH 464
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 187-516 4.97e-13

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 73.94  E-value: 4.97e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  187 ERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESapstngkrssdgsLSHEDLAKVLELQEVIDRQAREQS 266
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR-------------QISALRKDLARLEAEVEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  267 QMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLE 346
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  347 NEIANKDSMHRQTEDKNRQLQERLELAEQ---KLQQTLRKAET-LPEVEAELAQRVAALSKAEERHGNIEERLRQMEaql 422
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAeieELEELIEELESeLEALLNERASLEEALALLRSELEELSEELRELE--- 907

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  423 eEKNQELQRARQ--REKMNEEHNK--RLSDTVDKLLSESNERLQLHLkerMAALEDKNSLLREVENAKKQLEETQHDKDQ 498
Cdd:TIGR02168  908 -SKRSELRRELEelREKLAQLELRleGLEVRIDNLQERLSEEYSLTL---EEAEALENKIEDDEEEARRRLKRLENKIKE 983

                          330
                   ....*....|....*....
gi 1039778538  499 L-VVTIEALkAELEQMRLR 516
Cdd:TIGR02168  984 LgPVNLAAI-EEYEELKER 1001
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 990-1054 4.99e-13

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 64.98  E-value: 4.99e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039778538  990 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1054
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 74-462 8.48e-13

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 73.17  E-value: 8.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   74 ERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRmTVVKRQAQSPAG 153
Cdd:TIGR02168  678 EIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  154 VSS----EVEVLKALKSLFEHHKALDEK---VRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHE 226
Cdd:TIGR02168  756 LTEleaeIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  227 QESAPSTNGKRSSDGSLSHEDLAKVLE-LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQR 305
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEeLEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  306 EVREAMAQKEDMEERITTLEkrylaaQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQtlrkae 385
Cdd:TIGR02168  916 ELEELREKLAQLELRLEGLE------VRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE------ 983

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  386 tLPEVEAElaqrvaalskAEERHGNIEERLRQMEAQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDKLlsesNER 460
Cdd:TIGR02168  984 -LGPVNLA----------AIEEYEELKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTFDQV----NEN 1044


                   ..
gi 1039778538  461 LQ 462
Cdd:TIGR02168 1045 FQ 1046
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 54-432 1.07e-12

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 72.78  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   54 LRETQETLALTQGKLHEVGHERDSLQRQLNTAlpQEFAALTKELNvcREQLLEREEEIAELKAERNNTRLLLEHLECLVS 133
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELE 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  134 RHERSLrmtvvkrqaqspagvssevevlKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQk 213
Cdd:TIGR02168  257 ELTAEL----------------------QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN- 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  214 ktltdglLDGNHEQESAPSTNGKRSSDgsLSHEDLA----KVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTA 289
Cdd:TIGR02168  314 -------LERQLEELEAQLEELESKLD--ELAEELAeleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  290 RKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQER 369
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEA 462

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039778538  370 LELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRA 432
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 221-512 2.07e-12

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 72.02  E-value: 2.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  221 LDGNHEQESAPSTNGKRSSDG--SLSHEDLAKVLELQEVIDrqareqsQMKERLASLSSHAAELEEDLDTARKDLIKSEE 298
Cdd:TIGR02169  644 LEGELFEKSGAMTGGSRAPRGgiLFSRSEPAELQRLRERLE-------GLKRELSSLQSELRRIENRLDELSQELSDASR 716

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  299 MNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhRQTEDKNrQLQERLELAEQKLQ 378
Cdd:TIGR02169  717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE------ELEEDLH-KLEEALNDLEARLS 789

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  379 QtlrkaETLPEVEAElaqrvaaLSKAEERHGNIEERLRQMEAQLEEKNQELQRArqREKMNEEHNKRLS-----DTVDKL 453
Cdd:TIGR02169  790 H-----SRIPEIQAE-------LSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQRIDlkeqiKSIEKE 855

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039778538  454 LSESN---ERLQLHLKERMAALED----KNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQ 512
Cdd:TIGR02169  856 IENLNgkkEELEEELEELEAALRDlesrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 245-441 4.92e-12

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 67.26  E-value: 4.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  245 HEDLAKVLELQEvIDRQAReqsQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTL 324
Cdd:COG1579      3 PEDLRALLDLQE-LDSELD---RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  325 EKRylaaQREATSVHDLNDkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALSKA 404
Cdd:COG1579     79 EEQ----LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEK 143

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1039778538  405 EERhgnIEERLRQMEAQLEEKNQElqRARQREKMNEE 441
Cdd:COG1579    144 KAE---LDEELAELEAELEELEAE--REELAAKIPPE 175
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 155-672 1.14e-11

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.58  E-value: 1.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  155 SSEVEVLKALKSL--FEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAps 232
Cdd:COG1196    219 KEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-- 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  233 tngKRSSDGSLSHEdLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMA 312
Cdd:COG1196    297 ---LARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  313 QKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEA 392
Cdd:COG1196    373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---EAAE 449

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  393 ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdkllsESNERLQLHLKERMAAL 472
Cdd:COG1196    450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG-------FLEGVKAALLLAGLRGL 522

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  473 EDKNSLLREVENAKKQLEET----------QHDKDQLVVTIEALKAE---------LEQMRLRGPSLHHGRPHLGS---- 529
Cdd:COG1196    523 AGAVAVLIGVEAAYEAALEAalaaalqnivVEDDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGaavd 602

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  530 ------VPDFRFSVADGHVDAYSTSAVLRRPQKGRLAALRDEPSKVQTL------------------NEQDWERAQQASV 585
Cdd:COG1196    603 lvasdlREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLegeggsaggsltggsrreLLAALLEAEAELE 682

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  586 LANVAQAFESDVDVSDGEDDRDTLLSSVDLLSPSGQADAQTLAMMLQEQLDAINKEIRLIQEEKENTEQ---------RA 656
Cdd:COG1196    683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppDL 762

                          570
                   ....*....|....*...
gi 1039778538  657 EEIESRVGS--GSLDNLG 672
Cdd:COG1196    763 EELERELERleREIEALG 780
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
158-514 1.90e-11

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 68.53  E-value: 1.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  158 VEVLKALKSLFEHHkaldEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKR 237
Cdd:PRK02224   233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  238 SSDGSLSHEDLAKVL-ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKED 316
Cdd:PRK02224   309 AEAVEARREELEDRDeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  317 MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQklqqtLRKAETLPEVEAEL-- 394
Cdd:PRK02224   389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVeg 463

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  395 AQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLS--DTVDKLLSESNERLQ------LHLK 466
Cdd:PRK02224   464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEekreraEELR 543

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1039778538  467 ERMAALEDKNSLLREVenAKKQLEETQhDKDQLVVTIEALKAELEQMR 514
Cdd:PRK02224   544 ERAAELEAEAEEKREA--AAEAEEEAE-EAREEVAELNSKLAELKERI 588
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 874-938 3.29e-11

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188962  Cd Length: 64  Bit Score: 59.93  E-value: 3.29e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039778538  874 FAQWDGPTVVVWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 938
Cdd:cd09563      1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
mukB PRK04863
chromosome partition protein MukB;
179-508 5.10e-11

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 67.67  E-value: 5.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  179 RERLRVALERCSLLEEELGATHKELmiLKEQnnQKKTLTDGLLDGNHEQESAPSTNGKRSSDgslsHedLAKVLE---LQ 255
Cdd:PRK04863   278 ANERRVHLEEALELRRELYTSRRQL--AAEQ--YRLVEMARELAELNEAESDLEQDYQAASD----H--LNLVQTalrQQ 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  256 EVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEmntklqrEVREAMAQKEDMEERITTLEKR---YLAAQ 332
Cdd:PRK04863   348 EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEE-------EVDELKSQLADYQQALDVQQTRaiqYQQAV 420

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  333 REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQ-------------QTLRKAetLPEVEAELAQRVA 399
Cdd:PRK04863   421 QALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSvaqaahsqfeqayQLVRKI--AGEVSRSEAWDVA 498

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  400 --ALSKAEErHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDkllseSNERLQLHLKERMAALEDKNS 477
Cdd:PRK04863   499 reLLRRLRE-QRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD-----DEDELEQLQEELEARLESLSE 572

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1039778538  478 llrEVENAKKQLEETQHDKDQLVVTIEALKA 508
Cdd:PRK04863   573 ---SVSEARERRMALRQQLEQLQARIQRLAA 600
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 205-511 7.51e-11

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 66.68  E-value: 7.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  205 ILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVL---------------ELQEVIDRQAREQSQMK 269
Cdd:pfam15921  132 IRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMlshegvlqeirsilvDFEEASGKKIYEHDSMS 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  270 E-RLASLSSHAAELEEDLDTARKDLI--------KSEEMNTKLQREVREAMAQKEDMEER--------ITTLEKRYLAAQ 332
Cdd:pfam15921  212 TmHFRSLGSAISKILRELDTEISYLKgrifpvedQLEALKSESQNKIELLLQQHQDRIEQliseheveITGLTEKASSAR 291

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  333 REATSVHDLNDKLENEIANKDSMHRqtedknRQLQErLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAE------- 405
Cdd:pfam15921  292 SQANSIQSQLEIIQEQARNQNSMYM------RQLSD-LESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEltearte 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  406 -----ERHGNIEERLRQMEAQLEEKNQELQrarqrekMNEEHNKRLSD-------TVDKLLSESNER------------- 460
Cdd:pfam15921  365 rdqfsQESGNLDDQLQKLLADLHKREKELS-------LEKEQNKRLWDrdtgnsiTIDHLRRELDDRnmevqrleallka 437

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039778538  461 ----LQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELE 511
Cdd:pfam15921  438 mkseCQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 45-491 1.26e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 1.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG1196    337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  125 LEHLEcLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELM 204
Cdd:COG1196    417 ERLEE-ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  205 ILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEE 284
Cdd:COG1196    496 LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  285 DLdtaRKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEdKNR 364
Cdd:COG1196    576 FL---PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE-VTL 651

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  365 QLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNK 444
Cdd:COG1196    652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1039778538  445 RLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEE 491
Cdd:COG1196    732 AEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 44-513 1.43e-10

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 65.76  E-value: 1.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   44 LEERDRLLDTLR-ETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:TIGR00618  417 SAFRDLQGQLAHaKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  123 LLLEHLECLVSRHERSLRMTVVkrQAQSPAGVSSEVEvlkALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKE 202
Cdd:TIGR00618  497 LELQEEPCPLCGSCIHPNPARQ--DIDNPGPLTRRMQ---RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  203 LMILKEQNNQKKTLTDGLLdgNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQ--AREQSQMKERLASLSSHAA 280
Cdd:TIGR00618  572 FSILTQCDNRSKEDIPNLQ--NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQdvRLHLQQCSQELALKLTALH 649

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  281 ELEEDL------DTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDlNDKLENEIANKDS 354
Cdd:TIGR00618  650 ALQLTLtqervrEHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE-YDREFNEIENASS 728

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  355 MHRQTedknrqLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGnieERLRQMEAQLEEKNQELQRARQ 434
Cdd:TIGR00618  729 SLGSD------LAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTG---AELSHLAAEIQFFNRLREEDTH 799

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039778538  435 REKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQM 513
Cdd:TIGR00618  800 LLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 152-660 2.57e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 2.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  152 AGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQ---- 227
Cdd:COG1196    242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERleel 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  228 -ESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQRE 306
Cdd:COG1196    322 eEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  307 VREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIankdsmhRQTEDKNRQLQERLELAEQKLQQTLRKAEt 386
Cdd:COG1196    402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL-------EEAAEEEAELEEEEEALLELLAELLEEAA- 473

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  387 lpEVEAELAQRVAALSKAEERhgniEERLRQMEAQLEEKNQELQRARQREKMNEEHNK--RLSDTVDKLLSESNERLQLH 464
Cdd:COG1196    474 --LLEAALAELLEELAEAAAR----LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvaVLIGVEAAYEAALEAALAAA 547

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  465 LKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRPHLGSVPDFRFsvadGHVDA 544
Cdd:COG1196    548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL----GDTLL 623

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  545 YSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASVLANVAQAFESDVDVSDGEDDRDTLLSSVDLLSPSGQADA 624
Cdd:COG1196    624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703

                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1039778538  625 QTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIE 660
Cdd:COG1196    704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 267-514 3.02e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 3.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  267 QMKERLASLSSHAAELEEDLDtarkdlikseemntKLQREVREAmAQKEDMEERITTLEKRYLAAQREAtsVHDLNDKLE 346
Cdd:COG1196    183 ATEENLERLEDILGELERQLE--------------PLERQAEKA-ERYRELKEELKELEAELLLLKLRE--LEAELEELE 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  347 NEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHgniEERLRQMEAQLEEKN 426
Cdd:COG1196    246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL---EERRRELEERLEELE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  427 QELQRARQREKMNEEHNKRLSDTVDKL----------LSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDK 496
Cdd:COG1196    323 EELAELEEELEELEEELEELEEELEEAeeeleeaeaeLAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                          250
                   ....*....|....*...
gi 1039778538  497 DQLVVTIEALKAELEQMR 514
Cdd:COG1196    403 EELEEAEEALLERLERLE 420
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 272-519 4.22e-10

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 63.24  E-value: 4.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  272 LASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYlaaqreatsvhdlnDKLENEIAN 351
Cdd:COG4942     15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI--------------RALEQELAA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  352 KDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETL---PEVEAELAQR-VAALSKAEERHGNIEERLRQMEAQLEEKNQ 427
Cdd:COG4942     81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  428 ELQRARQREkmnEEHNKRLSDTVDKlLSESNERLQLHLKERMAALedkNSLLREVENAKKQLEETQHDKDQLVVTIEALK 507
Cdd:COG4942    161 ELAALRAEL---EAERAELEALLAE-LEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLE 233

                          250
                   ....*....|..
gi 1039778538  508 AELEQMRLRGPS 519
Cdd:COG4942    234 AEAAAAAERTPA 245
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
284-516 4.76e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.93  E-value: 4.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  284 EDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREAtsvhdlndkleNEIankdsmhrqtEDKN 363
Cdd:PRK03918   158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI-----------NEI----------SSEL 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  364 RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQ---LEEKNQELQRARQREKMNE 440
Cdd:PRK03918   217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKVKELKELKEKAEEYI 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  441 EHNKRLSDTVDKL------LSESNERLQlHLKERMAALEDKNSLLREVENAKKQLE---ETQHDKDQLVVTIEALKAELE 511
Cdd:PRK03918   297 KLSEFYEEYLDELreiekrLSRLEEEIN-GIEERIKELEEKEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELE 375


                   ....*
gi 1039778538  512 QMRLR 516
Cdd:PRK03918   376 RLKKR 380
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 246-511 5.66e-10

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 63.93  E-value: 5.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  246 EDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNtKLQREVREA-----MAQKEDMEER 320
Cdd:TIGR02169  160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREYegyelLKEKEALERQ 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  321 ITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhrQTEDKNRQLQERLELAEQKLQQTLRkaETLPEVEAELAQRVAA 400
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTEEISELEKRLE-------EIEQLLEELNKKIKDLGEEEQLRVK--EKIGELEAEIASLERS 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  401 LSKAEERHGNIEERLRQMEAQLEEKNQEL--------QRARQREKMNEEHnKRLSDTVDKLLSE------SNERLQLHLK 466
Cdd:TIGR02169  310 IAEKERELEDAEERLAKLEAEIDKLLAEIeelereieEERKRRDKLTEEY-AELKEELEDLRAEleevdkEFAETRDELK 388

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039778538  467 ERMAALED----KNSLLREVE---NAKKQLEETQHDKDQLVVTIEALKAELE 511
Cdd:TIGR02169  389 DYREKLEKlkreINELKRELDrlqEELQRLSEELADLNAAIAGIEAKINELE 440
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
152-491 7.53e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.54  E-value: 7.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  152 AGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLtDGLLDGNHEQESAP 231
Cdd:PRK03918   224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFY 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  232 STNGKRSSDGSlshEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQR----EV 307
Cdd:PRK03918   303 EEYLDELREIE---KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKK 379

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  308 REAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNRQLQERLELAEQKLQQTLRK-AE 385
Cdd:PRK03918   380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElKKAIEELKKAKGKCPVCGRELTEEHRKELLEEyTA 459

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  386 TLPEVEAELAQRVAALSKAEERHGNIEE---------RLRQMEAQLEEKNQELqrarqrEKMNEEHNKRLSDTVDKLLSE 456
Cdd:PRK03918   460 ELKRIEKELKEIEEKERKLRKELRELEKvlkkeseliKLKELAEQLKELEEKL------KKYNLEELEKKAEEYEKLKEK 533

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1039778538  457 SN--ERLQLHLKERMAALEDKNSLLREVENAKKQLEE 491
Cdd:PRK03918   534 LIklKGEIKSLKKELEKLEELKKKLAELEKKLDELEE 570
PTZ00121 PTZ00121
MAEBL; Provisional
 236-498 1.02e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 1.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  236 KRSSDGSLSHEDLAKVLELQEVID--RQAREQSQMKE-RLASLSSHAAELEEDLDTARKD-LIKSEEMntKLQREVREAM 311
Cdd:PTZ00121  1490 KKAEEAKKKADEAKKAAEAKKKADeaKKAEEAKKADEaKKAEEAKKADEAKKAEEKKKADeLKKAEEL--KKAEEKKKAE 1567

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  312 AQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTED---------KNRQLQERLELAEQKLQQTLR 382
Cdd:PTZ00121  1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKK 1647

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  383 KAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLlsesnERLQ 462
Cdd:PTZ00121  1648 KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELK 1722

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1039778538  463 LHLKERMAALEDknsLLREVENAKKQLEETQHDKDQ 498
Cdd:PTZ00121  1723 KAEEENKIKAEE---AKKEAEEDKKKAEEAKKDEEE 1755
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 110-512 1.64e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 1.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  110 EIAELKAErnntrlllehleclvsrherslrmtvVKRQAqspagvSSEVEVLKALKSLFEHHKALDEKVRERLRVALErc 189
Cdd:TIGR02168  678 EIEELEEK--------------------------IEELE------EKIAELEKALAELRKELEELEEELEQLRKELEE-- 723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  190 slLEEELGATHKELMIL-KEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQM 268
Cdd:TIGR02168  724 --LSRQISALRKDLARLeAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  269 KERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENE 348
Cdd:TIGR02168  802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  349 IAnkdsmhrqtedknrQLQERLELAEQKLQQtlrKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKnqe 428
Cdd:TIGR02168  882 RA--------------SLEEALALLRSELEE---LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL--- 941

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  429 LQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKER-------MAALEDKNSLLREVENAKKQLEETQHDKDQLVV 501
Cdd:TIGR02168  942 QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021

                          410
                   ....*....|.
gi 1039778538  502 TIEALKAELEQ 512
Cdd:TIGR02168 1022 AIEEIDREARE 1032
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 38-529 1.66e-09

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 62.37  E-value: 1.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   38 QLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHER--DSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELK 115
Cdd:TIGR00606  353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERqiKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR 432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  116 AERNNTRLLLEHLECLVSRHERSLRMtvVKRQAQSPAGVSSEV-----EVLKALK--SLFEHHKALDEKVRERLRVALER 188
Cdd:TIGR00606  433 DEKKGLGRTIELKKEILEKKQEELKF--VIKELQQLEGSSDRIleldqELRKAERelSKAEKNSLTETLKKEVKSLQNEK 510

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  189 CSLLEEElgatHKELMILKEQNNQKKTLTDGLL---DGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQ 265
Cdd:TIGR00606  511 ADLDRKL----RKLDQEMEQLNHHTTTRTQMEMltkDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEI 586

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  266 SQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQkEDMEERITTLEKRYLAAQREA---TSVHDLN 342
Cdd:TIGR00606  587 NQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQRamlAGATAVY 665

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  343 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAET-LPEVEAELA----QRVAALSKAEERHGNIEERLRQ 417
Cdd:TIGR00606  666 SQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKkkekRRDEMLGLAPGRQSIIDLKEKE 745

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  418 MEaQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN---------ERLQLHLKE------RMAALEDKNSLLREV 482
Cdd:TIGR00606  746 IP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKDverkiaQQAAKLQGSDLDRTV 824

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1039778538  483 ENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRPHLGS 529
Cdd:TIGR00606  825 QQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKS 871
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
254-520 3.91e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.23  E-value: 3.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  254 LQEVIdrqaREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRylaaQR 333
Cdd:PRK03918   167 LGEVI----KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KE 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  334 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQK---LQQTLRKAETLPEVEAELAQRVAALSKAEERHGN 410
Cdd:PRK03918   239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  411 IEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdklLSESNERLQ--LHLKERMAALEDKNSLLrEVENAKKQ 488
Cdd:PRK03918   319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-----LEERHELYEeaKAKKEELERLKKRLTGL-TPEKLEKE 392

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1039778538  489 LEETQHDKDQLVVTIEALKAELEQMRLRGPSL 520
Cdd:PRK03918   393 LEELEKAKEEIEEEISKITARIGELKKEIKEL 424
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 249-516 4.78e-09

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 60.08  E-value: 4.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  249 AKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY 328
Cdd:pfam19220   48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQL 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  329 LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERH 408
Cdd:pfam19220  128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDAT 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  409 gniEERLRQMEAQLEEKNQELQRA-RQREKMNEEHNKRLSdTVDKLLSESNERL----QLhLKERMAALEDKNSLLREVE 483
Cdd:pfam19220  208 ---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERA-SLRMKLEALTARAaateQL-LAEARNQLRDRDEAIRAAE 282

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1039778538  484 NAkkqLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:pfam19220  283 RR---LKEASIERDTLERRLAGLEADLERRTQQ 312
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 253-435 7.18e-09

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 59.39  E-value: 7.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYlAAQ 332
Cdd:COG4942     31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-AEL 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  333 REATSVHDLNDKLENEIANKD------------SMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAA 400
Cdd:COG4942    110 LRALYRLGRQPPLALLLSPEDfldavrrlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1039778538  401 LSKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 435
Cdd:COG4942    190 LEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 258-441 7.53e-09

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 59.07  E-value: 7.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  258 IDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREV----REAMAQKEDMEERITTLEKRYLAAQR 333
Cdd:COG3883     18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIdklqAEIAEAEAEIEERREELGERARALYR 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  334 ------------EATSVHDLNDKLE--NEI--ANKDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAET-LPEVEAEL 394
Cdd:COG3883     98 sggsvsyldvllGSESFSDFLDRLSalSKIadADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAaKAELEAQQ 177

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1039778538  395 AQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 441
Cdd:COG3883    178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 37-452 9.72e-09

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 9.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   37 EQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELnvcreqllEREEEIAELKA 116
Cdd:COG1196    413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--------LLEAALAELLE 484

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  117 ERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKslfehhKALDEKVRERLRVALERCSLLEEEL 196
Cdd:COG1196    485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE------AAYEAALEAALAAALQNIVVEDDEV 558

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  197 GATHKELmiLKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLS 276
Cdd:COG1196    559 AAAAIEY--LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  277 SHAAELEEDLDTARKDL-----------IKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKL 345
Cdd:COG1196    637 RRAVTLAGRLREVTLEGeggsaggsltgGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  346 ENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNI-----------EER 414
Cdd:COG1196    717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVnllaieeyeelEER 796

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1039778538  415 LRQMEAQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDK 452
Cdd:COG1196    797 YDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 45-441 1.11e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 59.70  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALpqEFAALTKELnvcreqlleREEEIAELKAERNNTRLL 124
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKEK---------REYEGYELLKEKEALERQ 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  125 LEHLECLVSRHERSLRmtvvKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKvrERLRValercsllEEELGATHKELM 204
Cdd:TIGR02169  239 KEAIERQLASLEEELE----KLTEEISELEKRLEEIEQLLEELNKKIKDLGEE--EQLRV--------KEKIGELEAEIA 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  205 ILKEQNNQKKtltdglldgnHEQESApstNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLAslsshaaELEE 284
Cdd:TIGR02169  305 SLERSIAEKE----------RELEDA---EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA-------ELKE 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  285 DLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNR 364
Cdd:TIGR02169  365 ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039778538  365 QLQERLELAEQKLQQTlrkaetlpeveaelaqrVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 441
Cdd:TIGR02169  445 DKALEIKKQEWKLEQL-----------------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 302-493 1.13e-08

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 58.69  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  302 KLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIankDSMHRQTEDKNRQLQERLELAEQKLQQTL 381
Cdd:COG3883     20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARALY 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  382 RKAETLPEVEA--------ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL 453
Cdd:COG3883     97 RSGGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1039778538  454 LSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 493
Cdd:COG3883    177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 315-582 1.27e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.69  E-value: 1.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  315 EDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQ-TLRKAETLPEVEAE 393
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQlEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  394 LAQRVAALSKAEErhgnieerLRQMEAQLEEKNQELQraRQREKMNEEHNkrlsdTVDKLLSESNERLQLHLKERMAALE 473
Cdd:TIGR02168  760 EAEIEELEERLEE--------AEEELAEAEAEIEELE--AQIEQLKEELK-----ALREALDELRAELTLLNEEAANLRE 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  474 DKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRPHLGSVPDFRFSVADGHVDAYSTSAVLRR 553
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1039778538  554 PQKGRLAALRDEPSKVQTLNEQ---DWERAQQ 582
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQlelRLEGLEV 936
PRK12704 PRK12704
phosphodiesterase; Provisional
 360-511 1.42e-08

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 59.02  E-value: 1.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  360 EDKNRQLQERLELAEQKLQQTLRKAETlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMN 439
Cdd:PRK12704    45 EEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039778538  440 EEHNKRLSDTVDKLLSESNERLqlhlkERMAAL---EDKNSLLREVEnakkqlEETQHDKDQLVVTIEAlKAELE 511
Cdd:PRK12704   123 QQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIEE-EAKEE 185
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 31-514 1.76e-08

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 58.98  E-value: 1.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   31 DADSHFEQLMVSMLEERDrlldTLRETQETLALTQGKLHEVGHERDSLQ----RQLNTALPQEFAALTKELNVCREQLLE 106
Cdd:pfam15921  167 DSNTQIEQLRKMMLSHEG----VLQEIRSILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  107 REEEIAELKAE-RNNTRLLLEH----LECLVSRHERSLR-MTVVKRQAQSPA-GVSSEVEV------------LKALKSL 167
Cdd:pfam15921  243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEITgLTEKASSARSQAnSIQSQLEIiqeqarnqnsmyMRQLSDL 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  168 FEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQ----KKTLTD---GLLDGNHEQESAPSTNGK---- 236
Cdd:pfam15921  323 ESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQfsqeSGNLDDqlqKLLADLHKREKELSLEKEqnkr 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  237 ---RSSDGSLSHEDLAKVL-------------------ELQEVIDRQAREQSQMKERLASLSSHAAELE----------E 284
Cdd:pfam15921  403 lwdRDTGNSITIDHLRRELddrnmevqrleallkamksECQGQMERQMAAIQGKNESLEKVSSLTAQLEstkemlrkvvE 482

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  285 DLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNR 364
Cdd:pfam15921  483 ELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDK 562

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  365 Q---LQERLELAEQKLQQTLRKAETL----PEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEknQELQRArqreK 437
Cdd:pfam15921  563 VieiLRQQIENMTQLVGQHGRTAGAMqvekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD--LELEKV----K 636

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  438 MNEEHNKRLSDTVDKllseSNERLQLhLKERMAALEDKNSLLREVE----NAKKQLEETQHDKDQLVVTIEALKAELEQM 513
Cdd:pfam15921  637 LVNAGSERLRAVKDI----KQERDQL-LNEVKTSRNELNSLSEDYEvlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711


                   .
gi 1039778538  514 R 514
Cdd:pfam15921  712 R 712
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 156-463 2.31e-08

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 58.60  E-value: 2.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  156 SEVEVLKALKSLFEHHKALDEKVR---------ERLRVA-------LERCSLLEEELGATHKEL----MILKEQNNQKkt 215
Cdd:pfam17380  266 TENEFLNQLLHIVQHQKAVSERQQqekfekmeqERLRQEkeekareVERRRKLEEAEKARQAEMdrqaAIYAEQERMA-- 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  216 ltdglLDGNHEQESAPSTNGKRSSDgSLSHEDLAKVLELQEVIDRQAREQSQMKERLaslsshaaelEEDLDTARKDLIK 295
Cdd:pfam17380  344 -----MERERELERIRQEERKRELE-RIRQEEIAMEISRMRELERLQMERQQKNERV----------RQELEAARKVKIL 407

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  296 SEEMNTKLQREVREAM--------AQKEDM----EERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN 363
Cdd:pfam17380  408 EEERQRKIQQQKVEMEqiraeqeeARQREVrrleEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK 487

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  364 RQLQERLELAEQKLQQtlRKAETLPE------VEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREK 437
Cdd:pfam17380  488 RAEEQRRKILEKELEE--RKQAMIEEerkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEER 565

                          330       340
                   ....*....|....*....|....*.
gi 1039778538  438 MNEEHNKRLSDTVDKLLSESNERLQL 463
Cdd:pfam17380  566 SRLEAMEREREMMRQIVESEKARAEY 591
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
44-468 2.75e-08

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.24  E-value: 2.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:COG4717     87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRELEEELE 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  123 LLLEHLECLVSRHERSLRmtvvkrqaqspagvSSEVEVLKALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGAT 199
Cdd:COG4717    167 ELEAELAELQEELEELLE--------------QLSLATEEELQDLAEELEELQQRLaelEEELEEAQEELEELEEELEQL 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  200 HKELMILKEQNNQKKTLTDGLLDGnheqeSAPSTNGKRSSDGSLSHEDLAKVLELQEVI-------DRQAREQSQMKERL 272
Cdd:COG4717    233 ENELEAAALEERLKEARLLLLIAA-----ALLALLGLGGSLLSLILTIAGVLFLVLGLLallflllAREKASLGKEAEEL 307

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  273 ASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANK 352
Cdd:COG4717    308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL 387

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  353 DSMHRQTEDKnRQLQERLELAEQKLQQ------TLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE--E 424
Cdd:COG4717    388 RAALEQAEEY-QELKEELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlE 466

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1039778538  425 KNQELQRARQREKMNEEHNKRLSD--TVDKLLSESNERLQLHLKER 468
Cdd:COG4717    467 EDGELAELLQELEELKAELRELAEewAALKLALELLEEAREEYREE 512
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
37-514 3.81e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.77  E-value: 3.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   37 EQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLqrqlnTALPQEFAALTKELNVCREQLLEREEEIAELKA 116
Cdd:PRK03918   199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI-----EELEKELESLEGSKRKLEEKIRELEERIEELKK 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  117 ERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpagVSSEVEvlKALKSLFEHHKALDEKVRErLRVALERCSLLEEEL 196
Cdd:PRK03918   274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLD---ELREIE--KRLSRLEEEINGIEERIKE-LEEKEERLEELKKKL 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  197 GATHKELMILKEQN---NQKKTLTDGLldgnheqesapstNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQ-SQMKERL 272
Cdd:PRK03918   348 KELEKRLEELEERHelyEEAKAKKEEL-------------ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEiSKITARI 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  273 ASLSSHAAELE---EDLDTA---------------RKDLIK--SEEMNtKLQREVREAMAQKEDMEERITTLEKrYLAAQ 332
Cdd:PRK03918   415 GELKKEIKELKkaiEELKKAkgkcpvcgrelteehRKELLEeyTAELK-RIEKELKEIEEKERKLRKELRELEK-VLKKE 492

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  333 REATSVHDLNDKLEN-----EIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEER 407
Cdd:PRK03918   493 SELIKLKELAEQLKEleeklKKYNLEELEKKAEEY-EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEE 571

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  408 HGNIEERLRQM----EAQLEEKNQELQR----------ARQREKMNEEHNKRLSDTVDKL---LSESNERLQlHLKERMA 470
Cdd:PRK03918   572 LAELLKELEELgfesVEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAfeeLAETEKRLE-ELRKELE 650

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039778538  471 ALEDKNS-------------LLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMR 514
Cdd:PRK03918   651 ELEKKYSeeeyeelreeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
PRK11281 PRK11281
mechanosensitive channel MscK;
314-514 7.52e-08

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 57.23  E-value: 7.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  314 KEDMEERITTLEKRYLAAQREATSVHDLNDKLEnEIANKDsmhrQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEA- 392
Cdd:PRK11281    38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  393 ELAQRVAALSkaeerhgnieerLRQMEAQLEEKNQELQRARqrekmneehnKRLSDTVDKLLSESN--ERLQLHLKERMA 470
Cdd:PRK11281   113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQAALYANSQ 170

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1039778538  471 ALEDKNSLLREVENAKKQLEETQhdKDQLVVTIEALKAELEQMR 514
Cdd:PRK11281   171 RLQQIRNLLKGGKVGGKALRPSQ--RVLLQAEQALLNAQNDLQR 212
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 353-514 8.50e-08

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.99  E-value: 8.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  353 DSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQEL-QR 431
Cdd:COG3883     15 DPQIQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgER 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  432 ARQREKmneehNKRLSDTVDKLL-SESNERL--QLHLKERMAalEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKA 508
Cdd:COG3883     92 ARALYR-----SGGSVSYLDVLLgSESFSDFldRLSALSKIA--DADADLLEELKADKAELEAKKAELEAKLAELEALKA 164


                   ....*.
gi 1039778538  509 ELEQMR 514
Cdd:COG3883    165 ELEAAK 170
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1077-1147 1.36e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.60  E-value: 1.36e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039778538  1077 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDfsalaLLLQIPTQNTQARAVLEREFNNLL 1147
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLK 66
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
246-435 1.38e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.08  E-value: 1.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  246 EDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLdtarkdlikseemntkLQREVREAMAQKEDMEERITTLE 325
Cdd:COG4913    252 ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL----------------LEAELEELRAELARLEAELERLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  326 KRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQkLQQTLRKAE-TLPEVEAELAQRVAAL--- 401
Cdd:COG4913    316 ARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEERERRRAR-LEALLAALGlPLPASAEEFAALRAEAaal 392

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1039778538  402 --------SKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 435
Cdd:COG4913    393 lealeeelEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
PTZ00121 PTZ00121
MAEBL; Provisional
 169-514 1.40e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.30  E-value: 1.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  169 EHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDglLDGNHEQESAPSTNGKRSSDGSLSHEDL 248
Cdd:PTZ00121  1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEA 1423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  249 AKVLELQEVIDrQAREQSQMKERLASLSSHAAELE--EDLDTARKDLIKSEEMNTKLQ--REVREAMAQKEDMEERITTL 324
Cdd:PTZ00121  1424 KKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKkaEEAKKKAEEAKKADEAKKKAEeaKKADEAKKKAEEAKKKADEA 1502

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  325 EKRYlAAQREATSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEA---ELAQRVAAL 401
Cdd:PTZ00121  1503 KKAA-EAKKKADEAKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKAEEKKKAEEakkAEEDKNMAL 1580

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  402 SKAEE----RHGNIEERLRQMEAQLEEKNQELQRARQ-----REKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAAL 472
Cdd:PTZ00121  1581 RKAEEakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1039778538  473 EDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMR 514
Cdd:PTZ00121  1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
32-509 1.56e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.08  E-value: 1.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   32 ADSHFEQLMVSMLEER-DRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-------LPQEFAALTKELNVCREQ 103
Cdd:COG4913    281 LRLWFAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqLEREIERLERELEERERR 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  104 LLEREEEIA-----------ELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSP--AGVSSEVEVLKALKSLFEH 170
Cdd:COG4913    361 RARLEALLAalglplpasaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelRELEAEIASLERRKSNIPA 440

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  171 HkalDEKVRERLRvalERCSLLEEEL---GathkELMILKEQ------------NNQKKTL------------------T 217
Cdd:COG4913    441 R---LLALRDALA---EALGLDEAELpfvG----ELIEVRPEeerwrgaiervlGGFALTLlvppehyaaalrwvnrlhL 510

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  218 DGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQareqsqmkerLASLSSHA-AELEEDLDTARKD---- 292
Cdd:COG4913    511 RGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAE----------LGRRFDYVcVDSPEELRRHPRAitra 580

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  293 -LIKSE----EMNTklQREVRE-------AMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLEN--EIANKDSMHRQ 358
Cdd:COG4913    581 gQVKGNgtrhEKDD--RRRIRSryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQErrEALQRLAEYSW 658

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  359 TEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRekm 438
Cdd:COG4913    659 DEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR--- 735

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039778538  439 neehnkrlsdtVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAE 509
Cdd:COG4913    736 -----------LEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
331-661 1.61e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.82  E-value: 1.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  331 AQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGN 410
Cdd:PRK02224   197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  411 IEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL----------LSESNERLQLH------LKERMAALED 474
Cdd:PRK02224   277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedrdeelrdrLEECRVAAQAHneeaesLREDADDLEE 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  475 KNSLLRE-VENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRgpsLHHGRPHLGSVPDFRFSVADGHVDAYSTSAVLRr 553
Cdd:PRK02224   357 RAEELREeAAELESELEEAREAVEDRREEIEELEEEIEELRER---FGDAPVDLGNAEDFLEELREERDELREREAELE- 432

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  554 pqkGRLAALRDEPSKVQTLNE--------QDWERAQQASVLANVAQAFES-DVDVSDGEDDRDTLLSSVDLLSPSGQADA 624
Cdd:PRK02224   433 ---ATLRTARERVEEAEALLEagkcpecgQPVEGSPHVETIEEDRERVEElEAELEDLEEEVEEVEERLERAEDLVEAED 509

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1039778538  625 QtlAMMLQEQLDAINKeirLIQEEKENTEQRAEEIES 661
Cdd:PRK02224   510 R--IERLEERREDLEE---LIAERRETIEEKRERAEE 541
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 253-513 2.35e-07

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 55.57  E-value: 2.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREamaqkedmeerittLEKRYLAAQ 332
Cdd:pfam01576  360 ELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE--------------LQARLSESE 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  333 REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQ--QTLRKAETLPEVeaelaqrvaalskaeerhgN 410
Cdd:pfam01576  426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQdtQELLQEETRQKL-------------------N 486

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  411 IEERLRQMEaqlEEKNQELQRARQREKMNEEHNKRLSdTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLE 490
Cdd:pfam01576  487 LSTRLRQLE---DERNSLQEQLEEEEEAKRNVERQLS-TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE 562

                          250       260
                   ....*....|....*....|...
gi 1039778538  491 ETQHDKDQLVVTIEALKAELEQM 513
Cdd:pfam01576  563 EKAAAYDKLEKTKNRLQQELDDL 585
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 45-512 2.37e-07

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 55.41  E-value: 2.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:TIGR04523  124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  125 LEHLECLVSRHeRSLRMTVVKRQAQSpagvSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL- 203
Cdd:TIGR04523  203 LSNLKKKIQKN-KSLESQISELKKQN----NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELe 277

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  204 ---MILKEQNNQKKTLTDGLLDGNHEQEsapstngkrssdgslshEDLAKvlELQEVIDRQAREQSQMKERLASLSSHAA 280
Cdd:TIGR04523  278 qnnKKIKELEKQLNQLKSEISDLNNQKE-----------------QDWNK--ELKSELKNQEKKLEEIQNQISQNNKIIS 338

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  281 ELEEDLDTARKDLIKSEEMNTKLQREVREamaqKEDMEERIttlekrylaaQREATSVHDLNDKLENEIANKDSMHRQTE 360
Cdd:TIGR04523  339 QLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKL----------KKENQSYKQEIKNLESQINDLESKIQNQE 404

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  361 DKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMN- 439
Cdd:TIGR04523  405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNl 484

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  440 EEHNKRLSDTVDKLLSESNERLQlhLKERMAALEDKNSLL----REVENAKKQLE------ETQHDKDQLVVTIEALKAE 509
Cdd:TIGR04523  485 EQKQKELKSKEKELKKLNEEKKE--LEEKVKDLTKKISSLkekiEKLESEKKEKEskisdlEDELNKDDFELKKENLEKE 562


                   ...
gi 1039778538  510 LEQ 512
Cdd:TIGR04523  563 IDE 565
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
113-516 2.49e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.07  E-value: 2.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  113 ELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPAGVSSEV-EVLKALKSLFEHHKALDEKVR--ERLRVALERC 189
Cdd:PRK03918   297 KLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHElyEEAKAKKEEL 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  190 SLLEEELGATHKELMI--LKEQNNQKKTLTDGLLD-----GNHEQESA---PSTNGKRSSDGS-------LSHEDLAKVL 252
Cdd:PRK03918   375 ERLKKRLTGLTPEKLEkeLEELEKAKEEIEEEISKitariGELKKEIKelkKAIEELKKAKGKcpvcgreLTEEHRKELL 454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  253 -ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARK--------DLIKS--EEMNTKLQREVREAMAQKEDMEERI 321
Cdd:PRK03918   455 eEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliklkelaEQLKEleEKLKKYNLEELEKKAEEYEKLKEKL 534

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  322 TTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQER-------LELAEQKLQQTLRKAETLPEVEAEL 394
Cdd:PRK03918   535 IKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveeLEERLKELEPFYNEYLELKDAEKEL 614

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  395 AQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQreKMNEEHNKRLSDTVDKL------LSESNERLQLHLKER 468
Cdd:PRK03918   615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELsrelagLRAELEELEKRREEI 692

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039778538  469 MAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIE---ALKAELEQMRLR 516
Cdd:PRK03918   693 KKTLEKLKEELEEREKAKKELEKLEKALERVEELREkvkKYKALLKERALS 743
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 874-940 3.35e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.45  E-value: 3.35e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039778538   874 FAQWDGPTVVVWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEI 940
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 999-1054 3.48e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.45  E-value: 3.48e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039778538   999 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1054
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
280-473 3.63e-07

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.39  E-value: 3.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  280 AELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQT 359
Cdd:COG4717     49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  360 ED--KNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLR-QMEAQLEEKNQELQRARQRE 436
Cdd:COG4717    129 PLyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRL 208

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039778538  437 KMNEEHNKRLSDTVDKLLSE----SNERLQLHLKERMAALE 473
Cdd:COG4717    209 AELEEELEEAQEELEELEEEleqlENELEAAALEERLKEAR 249
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
249-512 3.87e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 54.66  E-value: 3.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  249 AKVLELQEVIDRqAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRy 328
Cdd:PRK02224   489 EEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE- 566

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  329 laAQREATSVHDLNDKLEneiANKDSmhRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSkaeERH 408
Cdd:PRK02224   567 --AEEAREEVAELNSKLA---ELKER--IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR---ERK 636

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  409 GNIEERLRqmEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSE----SNERLQLH-LKERMAALEDKNSLLREVE 483
Cdd:PRK02224   637 RELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigavENELEELEeLRERREALENRVEALEALY 714

                          250       260
                   ....*....|....*....|....*....
gi 1039778538  484 NAKKQLEETQHDkdqlvvtieaLKAELEQ 512
Cdd:PRK02224   715 DEAEELESMYGD----------LRAELRQ 733
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
47-512 4.19e-07

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.39  E-value: 4.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   47 RDRLLDTLRETQETLALTQGKLHEVG-HERDSLQRQLNTA--LPQEFAALTKELNvcreqllEREEEIAELKAERNNTRL 123
Cdd:COG4717     44 RAMLLERLEKEADELFKPQGRKPELNlKELKELEEELKEAeeKEEEYAELQEELE-------ELEEELEELEAELEELRE 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  124 LLEHLECLVSRHERSLRMTVVKRQAQSPAGV-------------------SSEVEVLKALKSLFEHHKALDEKVRERLRV 184
Cdd:COG4717    117 ELEKLEKLLQLLPLYQELEALEAELAELPERleeleerleelreleeeleELEAELAELQEELEELLEQLSLATEEELQD 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  185 ALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLldgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQARE 264
Cdd:COG4717    197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQL-----ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSL 271

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  265 QSQMKERLASLSSHAAeleedldTARKDLIKSEEMNTKLQREVREAMAQKE-DMEERITTLEKRYLAAQREATSVHDLND 343
Cdd:COG4717    272 ILTIAGVLFLVLGLLA-------LLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLD 344

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  344 KleneIANKDSMHRQTEDKNRQLQerLELAEQKLQQTLRKAETlpEVEAELAQRVAALSKAEErhgnIEERLRQMEAQLE 423
Cdd:COG4717    345 R----IEELQELLREAEELEEELQ--LEELEQEIAALLAEAGV--EDEEELRAALEQAEEYQE----LKEELEELEEQLE 412

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  424 EKNQELQRARQREKmNEEHNKRLSDTVDKLLSESNERLQLH-----LKERMAALEDKNSL---LREVENAKKQLEETQHD 495
Cdd:COG4717    413 ELLGELEELLEALD-EEELEEELEELEEELEELEEELEELReelaeLEAELEQLEEDGELaelLQELEELKAELRELAEE 491

                          490
                   ....*....|....*..
gi 1039778538  496 KDQLVVTIEALKAELEQ 512
Cdd:COG4717    492 WAALKLALELLEEAREE 508
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
307-516 5.64e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 5.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  307 VREAMAQKEDMEERITTLE---KRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN--RQLQERLELAEQKLQQTL 381
Cdd:COG4913    213 VREYMLEEPDTFEAADALVehfDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAelEYLRAALRLWFAQRRLEL 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  382 RKAEtLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQ-----------LEEKNQELQRARQREKMNEEHNKRLSDTV 450
Cdd:COG4913    293 LEAE-LEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrleqLEREIERLERELEERERRRARLEALLAAL 371

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039778538  451 DKLLSESNERLQLHLKERMAALEDKNSLLREVEN----AKKQLEETQHDKDQLVVTIEALK-------AELEQMRLR 516
Cdd:COG4913    372 GLPLPASAEEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAEIASLErrksnipARLLALRDA 448
PTZ00121 PTZ00121
MAEBL; Provisional
 236-507 6.52e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 6.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  236 KRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKE 315
Cdd:PTZ00121  1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  316 DMEE--RITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAE 393
Cdd:PTZ00121  1310 KAEEakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  394 LAQRVAALSKAEERHGNIEERLRQMEA-----QLEEKNQELQRARQREKMNEEhnKRLSDTVDKLLSESN--ERLQLHLK 466
Cdd:PTZ00121  1390 KKKADEAKKKAEEDKKKADELKKAAAAkkkadEAKKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKkaEEAKKKAE 1467

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1039778538  467 ERMAA--LEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALK 507
Cdd:PTZ00121  1468 EAKKAdeAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
44-514 7.97e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.51  E-value: 7.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:PRK02224   250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  124 LLEhleclvsrhERSLRMTVVKRQAQSPAGVSSEVEvlKALKSLFEHHKALD---EKVRERLRVALERCSLLEEELGATH 200
Cdd:PRK02224   329 RLE---------ECRVAAQAHNEEAESLREDADDLE--ERAEELREEAAELEselEEAREAVEDRREEIEELEEEIEELR 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  201 KELMILKEQNNQKKTLTDGLLDgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVID----RQAREQSQMKERLASLS 276
Cdd:PRK02224   398 ERFGDAPVDLGNAEDFLEELRE---ERDELREREAELEATLRTARERVEEAEALLEAGKcpecGQPVEGSPHVETIEEDR 474

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  277 SHAAELEEDLDTARKDLiksEEMNTKLQR--EVREAMAQKEDMEERITTLEKRylAAQREATsVHDLNDKLENEIANKDS 354
Cdd:PRK02224   475 ERVEELEAELEDLEEEV---EEVEERLERaeDLVEAEDRIERLEERREDLEEL--IAERRET-IEEKRERAEELRERAAE 548

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  355 MHRQTEDKNRQLQERLELAEQKLqqtlrkaetlpEVEAELAQRVAALSKAEERHGNIEERLrqmeAQLEEKNQELQRARQ 434
Cdd:PRK02224   549 LEAEAEEKREAAAEAEEEAEEAR-----------EEVAELNSKLAELKERIESLERIRTLL----AAIADAEDEIERLRE 613

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  435 REK----MNEEHNKRLS---DTVDKLLSESNE-RLQlhlkermAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEAL 506
Cdd:PRK02224   614 KREalaeLNDERRERLAekrERKRELEAEFDEaRIE-------EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAV 686


                   ....*...
gi 1039778538  507 KAELEQMR 514
Cdd:PRK02224   687 ENELEELE 694
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 302-474 7.99e-07

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 51.46  E-value: 7.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  302 KLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLElaeqklqqTL 381
Cdd:COG1579     14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG--------NV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  382 RKAETLPEVEAELAQrvaalskAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERL 461
Cdd:COG1579     86 RNNKEYEALQKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158

                          170
                   ....*....|...
gi 1039778538  462 QLHLKERMAALED 474
Cdd:COG1579    159 EELEAEREELAAK 171
PTZ00121 PTZ00121
MAEBL; Provisional
 145-504 8.83e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 8.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  145 KRQAQSPAGVSSEVEVLKALKSLFEHHKALDE--KVRERLRVALERCSLLEEElgatHKELMILKEQNNQKKTLTDGLLD 222
Cdd:PTZ00121  1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakKKAEEAKKKADEAKKAAEA----KKKADEAKKAEEAKKADEAKKAE 1531

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  223 GNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVID-RQAREQSQMKERLASLSSHAAE---------LEEDLDTARKD 292
Cdd:PTZ00121  1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEaKKAEEDKNMALRKAEEAKKAEEarieevmklYEEEKKMKAEE 1611

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  293 LIKSEEMNTKLQrEVREAmaqkEDMEERITTLEKRYLAAQREATSVHDLNDklENEIANKDSMHRQTEDKNR--QLQERL 370
Cdd:PTZ00121  1612 AKKAEEAKIKAE-ELKKA----EEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIKAAEEAKKAEEDKKKaeEAKKAE 1684

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  371 ELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKrlsdtV 450
Cdd:PTZ00121  1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK-----I 1759

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039778538  451 DKLLSESNERLQLHLKERMAALEDKnsLLREVENAKKQLEETQHD-KDQLVVTIE 504
Cdd:PTZ00121  1760 AHLKKEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDKKIKDiFDNFANIIE 1812
PTZ00121 PTZ00121
MAEBL; Provisional
 260-663 8.91e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 8.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  260 RQAREQSQMKERLASLSSHAAELEEDLDTARK---DLIKSEEMNTKLQREVREAMAQKEDMEERittlEKRYLAAQREAT 336
Cdd:PTZ00121  1278 RKADELKKAEEKKKADEAKKAEEKKKADEAKKkaeEAKKADEAKKKAEEAKKKADAAKKKAEEA----KKAAEAAKAEAE 1353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  337 SVhdlNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQ--KLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEER 414
Cdd:PTZ00121  1354 AA---ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK 1430

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  415 LRQMEAQleEKNQELQRARQREKMNEEhnKRLSDTVDKLLSEsnerlqlhlKERMAALEDKNSLLREVENAKKQLEETQH 494
Cdd:PTZ00121  1431 KKADEAK--KKAEEAKKADEAKKKAEE--AKKAEEAKKKAEE---------AKKADEAKKKAEEAKKADEAKKKAEEAKK 1497

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  495 DKDQLVVTIEAlKAELEQMRlrgpslhhgrphlgsvpdfrfsvadgHVDAYSTSAVLRRPQKGRLAalrDEPSKVQTLNE 574
Cdd:PTZ00121  1498 KADEAKKAAEA-KKKADEAK--------------------------KAEEAKKADEAKKAEEAKKA---DEAKKAEEKKK 1547

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  575 QD----WERAQQASVLANVAQAFESdvdvsdgEDDRDTLLSSVDLLSPSGQADAQTLAMMLQEQLDAINKEIRLIQEEKE 650
Cdd:PTZ00121  1548 ADelkkAEELKKAEEKKKAEEAKKA-------EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620

                          410
                   ....*....|....*
gi 1039778538  651 NTEQ--RAEEIESRV 663
Cdd:PTZ00121  1621 KAEElkKAEEEKKKV 1635
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 999-1050 1.31e-06

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 46.46  E-value: 1.31e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039778538  999 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGI 1050
Cdd:cd09487      4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 38-513 1.35e-06

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 52.92  E-value: 1.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   38 QLMVSMLEERDR--LLDTLRETQETLALTQGKLHE--VGHERDSLQRQ-----LNTALPQEFAALTKELNvcreqlLERE 108
Cdd:pfam12128  231 QAIAGIMKIRPEftKLQQEFNTLESAELRLSHLHFgyKSDETLIASRQeerqeTSAELNQLLRTLDDQWK------EKRD 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  109 EEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKR---QAQSPAgVSSEVEVL-KALKSLFEHHKALDEKVRERLRV 184
Cdd:pfam12128  305 ELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKYNRRRSK 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  185 ALERCSlleEELGATHKELMILKEQNNQKKTLTDGLLDGnheQESApstngkrssdgsLSHEDLAKVLELQEVIDRQARE 264
Cdd:pfam12128  384 IKEQNN---RDIAGIKDKLAKIREARDRQLAVAEDDLQA---LESE------------LREQLEAGKLEFNEEEYRLKSR 445

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  265 QSQMKERLASLSSHAAELE------EDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSV 338
Cdd:pfam12128  446 LGELKLRLNQATATPELLLqlenfdERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDEL 525

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  339 --------HDLNDKLENEIAN-KDS---------MHR----------QTEDKNRQLQERLELAEQKLQQTLRKAETLpev 390
Cdd:pfam12128  526 elqlfpqaGTLLHFLRKEAPDwEQSigkvispelLHRtdldpevwdgSVGGELNLYGVKLDLKRIDVPEWAASEEEL--- 602

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  391 EAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLK---E 467
Cdd:pfam12128  603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDsanE 682

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039778538  468 RMAALE-DKNSLLREVENAKKQ-----LEETQHDKDQLVVTIEALKAELEQM 513
Cdd:pfam12128  683 RLNSLEaQLKQLDKKHQAWLEEqkeqkREARTEKQAYWQVVEGALDAQLALL 734
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 161-475 1.46e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.76  E-value: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  161 LKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSD 240
Cdd:TIGR02169  690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  241 GSLSHEDLAKVLE------LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQK 314
Cdd:TIGR02169  770 LEEDLHKLEEALNdlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  315 EDMEERITTLEKRYLAAQREA----TSVHDLNDKLEN---EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETL 387
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELEEELeeleAALRDLESRLGDlkkERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  388 PEVEAELAQRVAA----------LSKAEERHGNIEERLRQMEAQLEEKNQELqrarqrekmnEEHNKRLSDTVDKLLSES 457
Cdd:TIGR02169  930 EEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRALEPVNMLAIQEY----------EEVLKRLDELKEKRAKLE 999

                          330
                   ....*....|....*...
gi 1039778538  458 NERLQlhLKERMAALEDK 475
Cdd:TIGR02169 1000 EERKA--ILERIEEYEKK 1015
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
160-513 1.54e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  160 VLKALKSLFEhhKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESApstnGKRSS 239
Cdd:COG4717     39 LLAFIRAMLL--ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL----EAELE 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  240 DGSLSHEDLAKVLELQEVIDRQAREQSQMK---ERLASLSSHAA---ELEEDLDTARKDLIKSEEMNTKLQREVREAMAQ 313
Cdd:COG4717    113 ELREELEKLEKLLQLLPLYQELEALEAELAelpERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEE 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  314 K-EDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELA------------------- 373
Cdd:COG4717    193 ElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsli 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  374 ------------------------EQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIE-----------ERLRQM 418
Cdd:COG4717    273 ltiagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpeellelldriEELQEL 352

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  419 EAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL----------------LSESNERLQLHLKERMAALE--DKNSLLR 480
Cdd:COG4717    353 LREAEELEEELQLEELEQEIAALLAEAGVEDEEELraaleqaeeyqelkeeLEELEEQLEELLGELEELLEalDEEELEE 432

                          410       420       430
                   ....*....|....*....|....*....|...
gi 1039778538  481 EVENAKKQLEETQHDKDQLVVTIEALKAELEQM 513
Cdd:COG4717    433 ELEELEEELEELEEELEELREELAELEAELEQL 465
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 269-511 2.13e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.94  E-value: 2.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  269 KERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEK-------RYLAAQREATSVHDL 341
Cdd:TIGR04523   95 KDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKeleklnnKYNDLKKQKEELENE 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  342 NDKLENEIANKDSMHRQTEDKNRQLQERL---------------ELAEQKLQQTLRKaETLPEVEAELAQRVAALSKAEE 406
Cdd:TIGR04523  175 LNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkkiqknkslesQISELKKQNNQLK-DNIEKKQQEINEKTTEISNTQT 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  407 RHGNIEERLRQMEAQLEEKNQELQRArqrEKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENak 486
Cdd:TIGR04523  254 QLNQLKDEQNKIKKQLSEKQKELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQN-- 328

                          250       260
                   ....*....|....*....|....*
gi 1039778538  487 kQLEETQHDKDQLVVTIEALKAELE 511
Cdd:TIGR04523  329 -QISQNNKIISQLNEQISQLKKELT 352
PTZ00121 PTZ00121
MAEBL; Provisional
 246-509 2.47e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 2.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  246 EDLAKVLELQEVID-RQAREQSQMKERLASLSSHAAELEEDLDTARK-DLIKSEEMNTKLQREVREAMAQKEDMEERITT 323
Cdd:PTZ00121  1185 EEVRKAEELRKAEDaRKAEAARKAEEERKAEEARKAEDAKKAEAVKKaEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH 1264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  324 LEKRYLAAQ----REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQE--RLELAEQKLQQTLRKAETLPEvEAELAQR 397
Cdd:PTZ00121  1265 FARRQAAIKaeeaRKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKKADAAKK-KAEEAKK 1343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  398 VAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQlHLKERMAA------ 471
Cdd:PTZ00121  1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD-ELKKAAAAkkkade 1422

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1039778538  472 LEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAE 509
Cdd:PTZ00121  1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 224-498 4.30e-06

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 50.19  E-value: 4.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  224 NHEQESAPSTNGKRSSDGSL------SHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSE 297
Cdd:pfam15905   42 NNSKDASTPATARKVKSLELkkksqkNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLS 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  298 EMNTKLQREVREAMAQKEDMEE-----------RITTLEKRYLAAQREAT--SVHDLNDKLENEIANKDSMHRQTEDKNR 364
Cdd:pfam15905  122 ASVASLEKQLLELTRVNELLKAkfsedgtqkkmSSLSMELMKLRNKLEAKmkEVMAKQEGMEGKLQVTQKNLEHSKGKVA 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  365 QLQERLELAEQKLQQTlrKAETLpeveaELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNK 444
Cdd:pfam15905  202 QLEEKLVSTEKEKIEE--KSETE-----KLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELS 274

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039778538  445 RLSDTVD---KLLSESNERLQLHLKERmaaledKNSLLREVENAKKQL--EETQHDKDQ 498
Cdd:pfam15905  275 KQIKDLNekcKLLESEKEELLREYEEK------EQTLNAELEELKEKLtlEEQEHQKLQ 327
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 129-515 5.02e-06

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 50.66  E-value: 5.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  129 ECLVSRHErslrmtVVKRQAQSPAGVSSEVEVLKALKSLFEH-HKALDEKVrERLRVALERCSLLEEELGATHKELMILK 207
Cdd:pfam07888   38 ECLQERAE------LLQAQEAANRQREKEKERYKRDREQWERqRRELESRV-AELKEELRQSREKHEELEEKYKELSASS 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  208 EQNNQKKtltDGLLDGNHEQEsapstngkrssdgslshedlAKVLELQEVIdRQAREQSQMKErlaslsshaAELEEDLD 287
Cdd:pfam07888  111 EELSEEK---DALLAQRAAHE--------------------ARIRELEEDI-KTLTQRVLERE---------TELERMKE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  288 TARKDLIKSEE-------MNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLeNEIANKDSMHRQTE 360
Cdd:pfam07888  158 RAKKAGAQRKEeeaerkqLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL-TTAHRKEAENEALL 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  361 DKNRQLQERLELAEQKLqQTLRkaETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKN----QELQRARQRE 436
Cdd:pfam07888  237 EELRSLQERLNASERKV-EGLG--EELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRarwaQERETLQQSA 313

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039778538  437 KMNEEHNKRLSDTVDKLlsesNERLQlhlKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRL 515
Cdd:pfam07888  314 EADKDRIEKLSAELQRL----EERLQ---EERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQA 385
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
258-491 5.69e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 5.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  258 IDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATS 337
Cdd:COG4913    666 AEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  338 VH--DLNDKLENEIANK--DSMHRQTEDKNRQLQERLELAEQKLQQTLRKA-ETLPEVEAELAQRVAALSKAEERHGNIE 412
Cdd:COG4913    746 ELraLLEERFAAALGDAveRELRENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLPEYLALLDRLE 825

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039778538  413 erlrqmeaqleekNQELQRARQREKmneehnkrlsdtvdKLLSESNERLQLHLKERMAaledknsllREVENAKKQLEE 491
Cdd:COG4913    826 -------------EDGLPEYEERFK--------------ELLNENSIEFVADLLSKLR---------RAIREIKERIDP 868
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
253-456 6.28e-06

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 50.46  E-value: 6.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  253 ELQEVIDRQAREQSQMKERLASLSSHAAELE---------EDLDTARKDLIKSEEMNTKLQrEVREAMAQKED-MEERIT 322
Cdd:COG0497    169 ALKKELEELRADEAERARELDLLRFQLEELEaaalqpgeeEELEEERRRLSNAEKLREALQ-EALEALSGGEGgALDLLG 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  323 tlekrylAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQ----------ERLELAEQKLQ---QTLRK----AE 385
Cdd:COG0497    248 -------QALRALERLAEYDPSLAELAERLESALIELEEAASELRryldslefdpERLEEVEERLAllrRLARKygvtVE 320

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039778538  386 TLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQrekmneEHNKRLSDTVDKLLSE 456
Cdd:COG0497    321 ELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARK------KAAKKLEKAVTAELAD 385
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
399-516 8.65e-06

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 48.28  E-value: 8.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  399 AALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLlsesNERLQLHLK---ERMA--ALE 473
Cdd:COG1842     16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreALE 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1039778538  474 DKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:COG1842     92 RKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
341-524 8.83e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 8.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  341 LNDKLENEianKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQME- 419
Cdd:COG4717     47 LLERLEKE---ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEk 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  420 ---------------AQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVEN 484
Cdd:COG4717    124 llqllplyqelealeAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1039778538  485 AKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGR 524
Cdd:COG4717    204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 365-514 9.78e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.38  E-value: 9.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  365 QLQERLELAE--QKLQQTLRKAETLPEVEAELAQRVAALskaEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEh 442
Cdd:COG1579      5 DLRALLDLQEldSELDRLEHRLKELPAELAELEDELAAL---EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE- 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039778538  443 nkrlsdtvdKLLSESNERLQLHLKERMAALEDKNSLLREVE-NAKKQLEETQHDKDQLVVTIEALKAELEQMR 514
Cdd:COG1579     81 ---------QLGNVRNNKEYEALQKEIESLKRRISDLEDEIlELMERIEELEEELAELEAELAELEAELEEKK 144
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 36-438 9.92e-06

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 49.30  E-value: 9.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   36 FEQLMVSMLEERDRL--LDTLRE---------TQETLALTQGKLHEVGHERD-SLQRQLNTALPQEFAALTKELNVCREQ 103
Cdd:pfam19220    5 NELLRVRLGEMADRLedLRSLKAdfsqliepiEAILRELPQAKSRLLELEALlAQERAAYGKLRRELAGLTRRLSAAEGE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  104 LLEREEEIAELKAERNNTRLLLEHLECLVSrhERSLRMTVVKRQAqspagvSSEVEVLKALKslfEHHKALdekvRERLR 183
Cdd:pfam19220   85 LEELVARLAKLEAALREAEAAKEELRIELR--DKTAQAEALERQL------AAETEQNRALE---EENKAL----REEAQ 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  184 VALERCSLLEEELGATHKELMILKEQNNQKKTLTDglldgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEV--IDRQ 261
Cdd:pfam19220  150 AAEKALQRAEGELATARERLALLEQENRRLQALSE-------EQAAELAELTRRLAELETQLDATRARLRALEGqlAAEQ 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  262 AREQSQMKERLASLSSHAAE---LEEDLDTARKDLIKSEEMNTklqrevrEAMAQKEDMEERITTLEKRYLAAQREATSV 338
Cdd:pfam19220  223 AERERAEAQLEEAVEAHRAErasLRMKLEALTARAAATEQLLA-------EARNQLRDRDEAIRAAERRLKEASIERDTL 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  339 HDLNDKLENEIANKDSMHRQTEDKNRQLQERLElaeqklqqTLRKAetlpeveaeLAQRVAALSKAEERHGNIEERLRQM 418
Cdd:pfam19220  296 ERRLAGLEADLERRTQQFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIASLSDRIAEL 358

                          410       420
                   ....*....|....*....|....*..
gi 1039778538  419 E-------AQLEEKNQELQRARQREKM 438
Cdd:pfam19220  359 TkrfeverAALEQANRRLKEELQRERA 385
PRK01156 PRK01156
chromosome segregation protein; Provisional
 175-485 1.00e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 49.90  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  175 DEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDgLLDGNHEQESAPSTNGKRSSDGSLShEDLAKVLEL 254
Cdd:PRK01156   464 EEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE-YLESEEINKSINEYNKIESARADLE-DIKIKINEL 541

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  255 QEVIDRQareqSQMKERLASLSShaaeleEDLDTARKDLIKSeeMNTKLQREVREAMAQKEDMEERITTLEKRylaAQRE 334
Cdd:PRK01156   542 KDKHDKY----EEIKNRYKSLKL------EDLDSKRTSWLNA--LAVISLIDIETNRSRSNEIKKQLNDLESR---LQEI 606

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  335 ATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQErLELAEQKLQQTLrkaETLPEVEAELAQRVAALSKAEERHGNIEER 414
Cdd:PRK01156   607 EIGFPDDKSYIDKSIREIENEANNLNNKYNEIQE-NKILIEKLRGKI---DNYKKQIAEIDSIIPDLKEITSRINDIEDN 682

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039778538  415 LRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdkllSESNERLqlhlkERMAALEDKNSLLREVENA 485
Cdd:PRK01156   683 LKKSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETL-----ESMKKIKKAIGDLKRLREA 744
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
254-514 1.19e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  254 LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQR 333
Cdd:COG4372     29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  334 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEE 413
Cdd:COG4372    109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  414 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 493
Cdd:COG4372    189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268

                          250       260
                   ....*....|....*....|.
gi 1039778538  494 HDKDQLVVTIEALKAELEQMR 514
Cdd:COG4372    269 VEKDTEEEELEIAALELEALE 289
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 251-516 1.19e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 49.79  E-value: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  251 VLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEkryla 330
Cdd:pfam01576  140 ILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLE----- 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  331 aqREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLE---LAEQKLQQTLRKAET-LPEVEAELAQRVAALSKAEE 406
Cdd:pfam01576  215 --GESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEeetAQKNNALKKIRELEAqISELQEDLESERAARNKAEK 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  407 RHGNIEERLRQMEAQLEEK------NQELQRARQRE-----KMNEEHNKRLsdtvDKLLSESNERLQLHLKERMAALEDK 475
Cdd:pfam01576  293 QRRDLGEELEALKTELEDTldttaaQQELRSKREQEvtelkKALEEETRSH----EAQLQEMRQKHTQALEELTEQLEQA 368

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1039778538  476 NSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:pfam01576  369 KRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK 409
mukB PRK04863
chromosome partition protein MukB;
221-508 1.23e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.96  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  221 LDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDR--QAREQ----SQMKERLASLSSHAAELEEDLDTARKDli 294
Cdd:PRK04863   856 HESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRveEIREQldeaEEAKRFVQQHGNALAQLEPIVSVLQSD-- 933

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  295 ksEEMNTKLQREVREAMAQKEDMEERITTLEkrYLAAQREATSVHDLNDKLEneiankdsmhrQTEDKNRQLQERLELAE 374
Cdd:PRK04863   934 --PEQFEQLKQDYQQAQQTQRDAKQQAFALT--EVVQRRAHFSYEDAAEMLA-----------KNSDLNEKLRQRLEQAE 998

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  375 QklqQTLRKAETLPEVEAELAQRVAALSKAEERHgnieERLRQMEAQLEEKNQEL---------QRARQREkmnEEHNKR 445
Cdd:PRK04863   999 Q---ERTRAREQLRQAQAQLAQYNQVLASLKSSY----DAKRQMLQELKQELQDLgvpadsgaeERARARR---DELHAR 1068

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039778538  446 LSDTvdkllsesnerlqlhlKERMAALEDKNSLL-REVENAKKQLEETQHDKDQLVVTIEALKA 508
Cdd:PRK04863  1069 LSAN----------------RSRRNQLEKQLTFCeAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 249-484 1.42e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 49.66  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  249 AKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY 328
Cdd:TIGR00606  843 SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ 922

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  329 LAAQREATSVHDLNDKLENEIankdsmhRQTEDKNRQLQERLELAEQKLQQTlrKAETLPEVEAELAQRVAALSKAEERH 408
Cdd:TIGR00606  923 QEKEELISSKETSNKKAQDKV-------NDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQ 993

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039778538  409 GNIEERLRQMEAQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVEN 484
Cdd:TIGR00606  994 EKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHV 1071
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 127-485 1.67e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 49.20  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  127 HLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMIL 206
Cdd:pfam02463  676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  207 KEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDL 286
Cdd:pfam02463  756 RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEEL 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  287 DTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQL 366
Cdd:pfam02463  836 EELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK 915

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  367 QERLELAEQKLQQTLRKAETLPEVEaeLAQRVAALSKAEERHGNIEERLRQMEAQLEEK-----NQELQRARQREKMNEE 441
Cdd:pfam02463  916 ENEIEERIKEEAEILLKYEEEPEEL--LLEEADEKEKEENNKEEEEERNKRLLLAKEELgkvnlMAIEEFEEKEERYNKD 993

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1039778538  442 H--NKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENA 485
Cdd:pfam02463  994 EleKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFY 1039
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
44-434 2.18e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 2.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:COG4717    148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  124 LLEHLECLVSRHERSLRmtvVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL 203
Cdd:COG4717    228 ELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  204 MILKEQNNQKKTltdglldgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLAsLSSHAAELE 283
Cdd:COG4717    305 EELQALPALEEL----------EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIA 373

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  284 EDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSvhdlnDKLENEIANKDSMHRQTEDKN 363
Cdd:COG4717    374 ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEEL 448

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039778538  364 RQLQERLELAEQKLQQtLRKAETLPEVEAELAQRVAALSKAEERHGnieeRLRQMEAQLEEKNQELQRARQ 434
Cdd:COG4717    449 EELREELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWA----ALKLALELLEEAREEYREERL 514
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 253-383 3.10e-05

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 46.05  E-value: 3.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREA-MAQKEDMEERITTLEKRYLAA 331
Cdd:pfam15619   57 ELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDK 136

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039778538  332 QREatsVHDLNDKLEN-------EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 383
Cdd:pfam15619  137 DEK---IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 253-436 3.54e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.52  E-value: 3.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAmaqKEDMEERITTLEKRYLAAQ 332
Cdd:COG3883     20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERARALY 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  333 R------------EATSVHDLNDKLEN--------------------EIANKDSMHRQTEDKNRQLQERLELAEQKLQQT 380
Cdd:COG3883     97 RsggsvsyldvllGSESFSDFLDRLSAlskiadadadlleelkadkaELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  381 LRKAE----TLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRE 436
Cdd:COG3883    177 QAEQEallaQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
259-434 3.67e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.09  E-value: 3.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  259 DRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIK----------SEEMNTKLQR------EVREAMAQKEDMEERIT 322
Cdd:COG3206    164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQQlselesQLAEARAELAEAEARLA 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  323 TLEKR------YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN---RQLQERLELAEQKLQQTLRKAETLPEVEAE 393
Cdd:COG3206    244 ALRAQlgsgpdALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEAELE 323

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1039778538  394 -LAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQ 434
Cdd:COG3206    324 aLQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 379-512 4.30e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.46  E-value: 4.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  379 QTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNE----EHNKRLSDTVDKLL 454
Cdd:COG1579      4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEleieEVEARIKKYEEQLG 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039778538  455 SESNER----LQL---HLKERMAALEDK-NSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQ 512
Cdd:COG1579     84 NVRNNKeyeaLQKeieSLKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1077-1147 4.40e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 42.64  E-value: 4.40e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039778538 1077 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFsalalLLQIPTQNTQARAVLEREFNNLL 1147
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLED-----LKRLGITSVGHRRKILKKIQELK 66
RNase_Y_N pfam12072
RNase Y N-terminal region;
364-511 5.78e-05

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 45.65  E-value: 5.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  364 RQLQERLELAEQKLQQTLRKAETLP----------------EVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQ 427
Cdd:pfam12072   27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  428 ELQRARQREKMNEEHNKRLSDTVDKLLSESNERLqlhlkERMAAL---EDKNSLLREVEnakkqlEETQHDKDQLVVTIE 504
Cdd:pfam12072  107 SLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIE 175


                   ....*..
gi 1039778538  505 AlKAELE 511
Cdd:pfam12072  176 E-EAKEE 181
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 253-507 7.91e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.94  E-value: 7.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKS-------EEMNTKLQREVREAMAQKEDMEERITTLE 325
Cdd:TIGR04523  395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNnseikdlTNQDSVKELIIKNLDNTRESLETQLKVLS 474

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  326 KRYLAAQREAtsvhdlnDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpevEAELAQRVAALSKAE 405
Cdd:TIGR04523  475 RSINKIKQNL-------EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL---ESEKKEKESKISDLE 544

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  406 ERHGNIEERLR--QMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNE-RLQLHLKERMAA-LED------- 474
Cdd:TIGR04523  545 DELNKDDFELKkeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDlIKEIEEKEKKISsLEKelekakk 624

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1039778538  475 ---------------KNSLLREVENAKKQLEETQHDKDQLVVTIEALK 507
Cdd:TIGR04523  625 eneklssiiknikskKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESK 672
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
363-502 1.03e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 45.81  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  363 NRQLQERLELAEQKLQQtlrkaetlpeVEAELAqRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQ-------- 434
Cdd:COG1566     78 PTDLQAALAQAEAQLAA----------AEAQLA-RLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQAlykkgavs 146

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039778538  435 REKMNEEHNKRlsDTVDKLLSESNERLQLhLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVT 502
Cdd:COG1566    147 QQELDEARAAL--DAAQAQLEAAQAQLAQ-AQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIR 211
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 281-521 1.12e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.50  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  281 ELEEDLDTARKDLIKSEEMNTKlqREVREAMAQKEDMEERI----TTLEKRYLAAQREATSVHDLNDKLENEIANKDSMH 356
Cdd:pfam02463  157 EIEEEAAGSRLKRKKKEALKKL--IEETENLAELIIDLEELklqeLKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  357 RQTEDKNRQLQERLELAEQKLQQTLRKAEtlpevEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRE 436
Cdd:pfam02463  235 NEERIDLLQELLRDEQEEIESSKQEIEKE-----EEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  437 KMNEEhNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:pfam02463  310 VDDEE-KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388


                   ....*
gi 1039778538  517 GPSLH 521
Cdd:pfam02463  389 AAKLK 393
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 164-658 1.16e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.64  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  164 LKSLFEHHKALDEKVrERLRVALERC----SLLEEELGATHKELMILKEQnnqkktltdglldgnhEQESAPSTNGKRSS 239
Cdd:pfam05483  284 LKELIEKKDHLTKEL-EDIKMSLQRSmstqKALEEDLQIATKTICQLTEE----------------KEAQMEELNKAKAA 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  240 DGSLSHEDLAKVLELQEVI----DRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKL--QREVREAMAQ 313
Cdd:pfam05483  347 HSFVVTEFEATTCSLEELLrteqQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILaeDEKLLDEKKQ 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  314 KEDMEERITTLEKR--YLAAQREaTSVHDLNDKLENEIANKDSMHRQTEDKNRQLQ-ERLELAEQKLQQTLRKAETlPEV 390
Cdd:pfam05483  427 FEKIAEELKGKEQEliFLLQARE-KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEkEKLKNIELTAHCDKLLLEN-KEL 504

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  391 EAELAQRVAALSKAEERHGNIEERLRQMEAQLEE-KNQELQRARQREKMNEEHnKRLSDTVDKLLSESNERLQLHLKERM 469
Cdd:pfam05483  505 TQEASDMTLELKKHQEDIINCKKQEERMLKQIENlEEKEMNLRDELESVREEF-IQKGDEVKCKLDKSEENARSIEYEVL 583

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  470 AALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALK----AELEQMRLRGPSLHHGRPHLGSVPDFRFSVADGH---- 541
Cdd:pfam05483  584 KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgsAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYqkei 663

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  542 -VDAYSTSAVLRRPQKGRLAAlrDEPSKVQtlNEQDWERAQQASVLANVAQAFESDVD-VSDGEDDRDTLLSSVDLLSPS 619
Cdd:pfam05483  664 eDKKISEEKLLEEVEKAKAIA--DEAVKLQ--KEIDKRCQHKIAEMVALMEKHKHQYDkIIEERDSELGLYKNKEQEQSS 739

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1039778538  620 GQADAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEE 658
Cdd:pfam05483  740 AKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 320-516 1.37e-04

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 44.98  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  320 RITTLEKRYLAAQREATSVHDLNDKLENeIANKDSmhrqTEDKNRQLQERLELAEQKLQQTLRKAETL------------ 387
Cdd:pfam12795    1 KLDELEKAKLDEAAKKKLLQDLQQALSL-LDKIDA----SKQRAAAYQKALDDAPAELRELRQELAALqakaeaapkeil 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  388 -----PEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTvDKLLSESnerLQ 462
Cdd:pfam12795   76 aslslEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPP-GEPLSEA---QR 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039778538  463 LHLKERMAALEDKNSLLR-EVENA-------KKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:pfam12795  152 WALQAELAALKAQIDMLEqELLSNnnrqdllKARRDLLTLRIQRLEQQLQALQELLNEKRLQ 213
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 249-513 1.62e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.94  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  249 AKVLELQEVIDRQAR-EQSQMKERLASLSSHAAELEEDLDTARK---DLIKS----EEMNTKLQREVREAMAQKEDMEER 320
Cdd:pfam01576  327 QEVTELKKALEEETRsHEAQLQEMRQKHTQALEELTEQLEQAKRnkaNLEKAkqalESENAELQAELRTLQQAKQDSEHK 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  321 -------ITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN-----------RQLQERLELAEQKLQQTLR 382
Cdd:pfam01576  407 rkklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNiklskdvssleSQLQDTQELLQEETRQKLN 486

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  383 KAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL--------- 453
Cdd:pfam01576  487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALtqqleekaa 566

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  454 ----LSESNERLQLHLKERMAALEDKNSLLREVENAKKQ---------------------------------------LE 490
Cdd:pfam01576  567 aydkLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKfdqmlaeekaisaryaeerdraeaeareketralslaraLE 646

                          330       340
                   ....*....|....*....|...
gi 1039778538  491 ETQHDKDQLVVTIEALKAELEQM 513
Cdd:pfam01576  647 EALEAKEELERTNKQLRAEMEDL 669
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 246-494 1.65e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 46.12  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  246 EDLAKVLELQevidRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLE 325
Cdd:TIGR00618  273 RAQEAVLEET----QERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  326 KRYLAAQReatsvhdLNDKLENEIANKDSMHRQTEDKN--RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS- 402
Cdd:TIGR00618  349 TLHSQEIH-------IRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRd 421

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  403 -KAEERHGNIEERLRQMEAQLEEknQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLRE 481
Cdd:TIGR00618  422 lQGQLAHAKKQQELQQRYAELCA--AAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLEL 499

                          250
                   ....*....|...
gi 1039778538  482 VENAKKQLEETQH 494
Cdd:TIGR00618  500 QEEPCPLCGSCIH 512
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 248-514 1.81e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.10  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  248 LAKVLELQEVIDR--QAREQ-SQMKERLASLSSH---AAELEEDLDTARKDLIKSEEmntkLQREVREAMAQKEDMEERI 321
Cdd:COG3096    882 QANLLADETLADRleELREElDAAQEAQAFIQQHgkaLAQLEPLVAVLQSDPEQFEQ----LQADYLQAKEQQRRLKQQI 957

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  322 TTLEkrYLAAQREATSVHDLNDKLEneiankdsmhrQTEDKNRQLQERLELAEQklqqtlrkaetlpeveaelaqrvaAL 401
Cdd:COG3096    958 FALS--EVVQRRPHFSYEDAVGLLG-----------ENSDLNEKLRARLEQAEE------------------------AR 1000

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  402 SKAEERhgnieerLRQMEAQLEEKNQELQ----RARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNS 477
Cdd:COG3096   1001 REAREQ-------LRQAQAQYSQYNQVLAslksSRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELHEELSQNRS 1073

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1039778538  478 LLREVEnakKQLEETQHDKDQLVVTIEALKAELEQMR 514
Cdd:COG3096   1074 RRSQLE---KQLTRCEAEMDSLQKRLRKAERDYKQER 1107
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
999-1054 1.88e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 40.72  E-value: 1.88e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039778538  999 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLrGQLKMVDSFHRNSFQCGIMCLR 1054
Cdd:pfam07647   11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDL-KRLGITSVGHRRKILKKIQELK 66
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 877-935 1.97e-04

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.


Pssm-ID: 188903  Cd Length: 74  Bit Score: 40.78  E-value: 1.97e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039778538  877 WDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 935
Cdd:cd09504      5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
250-421 2.01e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  250 KVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQR--EVREAMAQKEDMEERITTLEKR 327
Cdd:COG3206    206 GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSAR 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  328 YLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEE 406
Cdd:COG3206    286 YTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365

                          170
                   ....*....|....*
gi 1039778538  407 RHGNIEERLRQMEAQ 421
Cdd:COG3206    366 LYESLLQRLEEARLA 380
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 342-446 2.38e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.59  E-value: 2.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  342 NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRV-----AALSKAEERHGNIEERLR 416
Cdd:PRK00409   515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqQAIKEAKKEADEIIKELR 594

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1039778538  417 QMEAQL--EEKNQELQRARQR-EKMNEEHNKRL 446
Cdd:PRK00409   595 QLQKGGyaSVKAHELIEARKRlNKANEKKEKKK 627
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 36-497 2.80e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 45.34  E-value: 2.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   36 FEQLMVSMLEERDRLLDTLRETQ--ETLALTQGKLHEVGH-ERDSLQRQ---LNTALPQEFAALTKELNVCREQLLEREE 109
Cdd:TIGR00618  154 FAQFLKAKSKEKKELLMNLFPLDqyTQLALMEFAKKKSLHgKAELLTLRsqlLTLCTPCMPDTYHERKQVLEKELKHLRE 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  110 EIAELKAERNNTRLLLEHLECLVSRHE--RSLRMTVVKRQAQSPAGVSSEVEVLKALKS--LFEHHKALDEKVRERLRVA 185
Cdd:TIGR00618  234 ALQQTQQSHAYLTQKREAQEEQLKKQQllKQLRARIEELRAQEAVLEETQERINRARKAapLAAHIKAVTQIEQQAQRIH 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  186 LERCSLLEEELGATHKELMILKEQNN--QKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDrQAR 263
Cdd:TIGR00618  314 TELQSKMRSRAKLLMKRAAHVKQQSSieEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKT-TLT 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  264 EQSQMKERLASLSSHAAELEEDLDTARKDL---IKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATsvhd 340
Cdd:TIGR00618  393 QKLQSLCKELDILQREQATIDTRTSAFRDLqgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL---- 468

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  341 lnDKLENEIANKDSMHRQTEDKNRQLQERLELaEQKLQQTLRKAETLPEVEAELAQRVAALS----KAEERHGNIEERLR 416
Cdd:TIGR00618  469 --KEREQQLQTKEQIHLQETRKKAVVLARLLE-LQEEPCPLCGSCIHPNPARQDIDNPGPLTrrmqRGEQTYAQLETSEE 545

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  417 QMEAQL-EEKNQ------ELQRARQREKMNEEHNKRLSDTVDKLLSEsnerLQLHLKERMAALEDKNSLLREVENAKKQL 489
Cdd:TIGR00618  546 DVYHQLtSERKQraslkeQMQEIQQSFSILTQCDNRSKEDIPNLQNI----TVRLQDLTEKLSEAEDMLACEQHALLRKL 621


                   ....*...
gi 1039778538  490 EETQHDKD 497
Cdd:TIGR00618  622 QPEQDLQD 629
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 163-441 2.95e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 45.20  E-value: 2.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  163 ALKSLFEhhkALDEKVR--ERLRVALER-CSLLEEELGATHKELMILKEQ-NNQKKTLTD---GLLD-GNHEQESAPSTN 234
Cdd:pfam10174  437 ALTTLEE---ALSEKERiiERLKEQREReDRERLEELESLKKENKDLKEKvSALQPELTEkesSLIDlKEHASSLASSGL 513

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  235 GKRSSDGSL-----SHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHaaeLEEDLDTARKDLIKSEEMNTKLQREVRE 309
Cdd:pfam10174  514 KKDSKLKSLeiaveQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRL---LEQEVARYKEESGKAQAEVERLLGILRE 590

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  310 AMAQKEDMEERITTLEKRYLAAQREATSvhdlndklenEIANKDSMhrQTEDKNRQLQErlelaeqkLQQTLRKAETLPE 389
Cdd:pfam10174  591 VENEKNDKDKKIAELESLTLRQMKEQNK----------KVANIKHG--QQEMKKKGAQL--------LEEARRREDNLAD 650

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039778538  390 VEAE--LAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQ-REKMNEE 441
Cdd:pfam10174  651 NSQQlqLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAeRRKQLEE 705
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 45-427 3.33e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 45.33  E-value: 3.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   45 EERDRLLD-------TLRETQETLALTQGKLHEVGHERDSLQRQlNTALPQEFAALTKELNVCREQLLER------EEEI 111
Cdd:COG3096    278 NERRELSEralelrrELFGARRQLAEEQYRLVEMARELEELSAR-ESDLEQDYQAASDHLNLVQTALRQQekieryQEDL 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  112 AELkAERnntrlLLEHLECLVSRHERSLRmtvvkRQAQSPAgvsSEVEVlKALKS-LFEHHKALDE---------KVRER 181
Cdd:COG3096    357 EEL-TER-----LEEQEEVVEEAAEQLAE-----AEARLEA---AEEEV-DSLKSqLADYQQALDVqqtraiqyqQAVQA 421

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  182 LRVALERCSLLEEELGATHKELMILKEQNNQkktLTDGLLDGNHeqesapstngkRSSDGSLSHEDLAKVLELQEVID-- 259
Cdd:COG3096    422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQ---ATEEVLELEQ-----------KLSVADAARRQFEKAYELVCKIAge 487

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  260 --------------RQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAmaqkEDMEERITTLE 325
Cdd:COG3096    488 versqawqtarellRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA----EELEELLAELE 563

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  326 krylaAQREatsvhDLNDKLENEIANKDSMHRQTEDKNRQ-------------LQERLE-LAEQkLQQTLrkaETLPEVE 391
Cdd:COG3096    564 -----AQLE-----ELEEQAAEAVEQRSELRQQLEQLRARikelaarapawlaAQDALErLREQ-SGEAL---ADSQEVT 629

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1039778538  392 AELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQ 427
Cdd:COG3096    630 AAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 267-430 3.34e-04

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 42.64  E-value: 3.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  267 QMKERLASLSSHAAELEEDLDTARKDLIK---------SEEMNTKLQrEVREAMAQK-EDMEERIT-TLEKrylAAQREA 335
Cdd:pfam01442    1 LLEDSLDELSTYAEELQEQLGPVAQELVDrleketealRERLQKDLE-EVRAKLEPYlEELQAKLGqNVEE---LRQRLE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  336 TSVHDLNDKLENEIankDSMHRQTEDKNRQLQERLELAEQKLQQTLrkAETLPEVEAELAQRVAALSK-----AEERHGN 410
Cdd:pfam01442   77 PYTEELRKRLNADA---EELQEKLAPYGEELRERLEQNVDALRARL--APYAEELRQKLAERLEELKEslapyAEEVQAQ 151

                          170       180
                   ....*....|....*....|
gi 1039778538  411 IEERLRQMEAQLEEKNQELQ 430
Cdd:pfam01442  152 LSQRLQELREKLEPQAEDLR 171
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 176-517 3.59e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 44.73  E-value: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  176 EKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLldGNHEQESAPSTNgkrssdgslSHEDLAKVLELQ 255
Cdd:pfam05557  135 EELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEI--QSQEQDSEIVKN---------SKSELARIPELE 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  256 EVIDRQAREQSQ---MKERLASLSSHAAELEEDLDT---ARKDLIKSEEMNTKLQREVRE----------AMAQKEDMEE 319
Cdd:pfam05557  204 KELERLREHNKHlneNIENKLLLKEEVEDLKRKLEReekYREEAATLELEKEKLEQELQSwvklaqdtglNLRSPEDLSR 283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  320 RITTLEKRYLAAQREATSVhdlndkleneiankDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVA 399
Cdd:pfam05557  284 RIEQLQQREIVLKEENSSL--------------TSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVL 349

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  400 ALSKaeERHGnIEERLRQMEAQLEEKN---QELQRARQREKMNEE---HNKRLSDTVDKLLSE--------SNERLQLHL 465
Cdd:pfam05557  350 LLTK--ERDG-YRAILESYDKELTMSNyspQLLERIEEAEDMTQKmqaHNEEMEAQLSVAEEElggykqqaQTLERELQA 426

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039778538  466 KERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRG 517
Cdd:pfam05557  427 LRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQG 478
PTZ00121 PTZ00121
MAEBL; Provisional
 295-512 3.83e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 3.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  295 KSEEMNTKLQREVREAMAQKED---MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERLE 371
Cdd:PTZ00121  1105 KTETGKAEEARKAEEAKKKAEDarkAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDA-KKAEAARK 1183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  372 LAEQKLQQTLRKAETLPEVEA----------------ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRAR-- 433
Cdd:PTZ00121  1184 AEEVRKAEELRKAEDARKAEAarkaeeerkaeearkaEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARma 1263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  434 ---QREKMNEEHNKRLSDTVDKL--------LSESNERLQL-HLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVV 501
Cdd:PTZ00121  1264 hfaRRQAAIKAEEARKADELKKAeekkkadeAKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK 1343

                          250
                   ....*....|.
gi 1039778538  502 TIEALKAELEQ 512
Cdd:PTZ00121  1344 AAEAAKAEAEA 1354
46 PHA02562
endonuclease subunit; Provisional
 281-500 4.28e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 44.62  E-value: 4.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  281 ELEEDLDT--ARKDLIKSE-EMNTKLQREVREAMAQkedmeeRITTLEKRYLAAQREATSVHDLNDKLENEIANKD-SMH 356
Cdd:PHA02562   178 ELNQQIQTldMKIDHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLNLVmDIE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  357 RQTEDKNRQLQERLELAEQ-----KLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQ-MEAQLEEKNQELQ 430
Cdd:PHA02562   252 DPSAALNKLNTAAAKIKSKieqfqKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKlDTAIDELEEIMDE 331

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039778538  431 RARQREKMNEEHNK-RLSDTVDKLLSESNERLQLHLKERMAALEDKNSllrEVENAKKQLEETQHDKDQLV 500
Cdd:PHA02562   332 FNEQSKKLLELKNKiSTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE---ELAKLQDELDKIVKTKSELV 399
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 264-428 4.40e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 42.97  E-value: 4.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  264 EQSQMKERLASLSSHAAELEEDLDTARKD---LIKSEEMNTKLQREVREAMAQKEDMEERIttlekrylaaqreatsvhd 340
Cdd:pfam13851   55 ENKRLTEPLQKAQEEVEELRKQLENYEKDkqsLKNLKARLKVLEKELKDLKWEHEVLEQRF------------------- 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  341 lnDKLENEianKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK-AETLPEVEAELAQRVAALSKAEERHGNIEERLRQMe 419
Cdd:pfam13851  116 --EKVERE---RDELYDKFEAAIQDVQQKTGLKNLLLEKKLQAlGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDV- 189


                   ....*....
gi 1039778538  420 aqLEEKNQE 428
Cdd:pfam13851  190 --LESKNQL 196
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 193-514 4.67e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.78  E-value: 4.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  193 EEELGATHKELMILKEQNNQ-KKTLTDglLDGNHEQESAPST--NGKRSSDGSLSHED-------LAKVLELQEVI---- 258
Cdd:pfam01576    4 EEEMQAKEEELQKVKERQQKaESELKE--LEKKHQQLCEEKNalQEQLQAETELCAEAeemrarlAARKQELEEILhele 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  259 ----DRQAREQSQMKERlASLSSHAAELEEDLD---TARK------------------DLIKSEEMNTKLQREvreamaq 313
Cdd:pfam01576   82 srleEEEERSQQLQNEK-KKMQQHIQDLEEQLDeeeAARQklqlekvtteakikkleeDILLLEDQNSKLSKE------- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  314 KEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQtEDKNRQLQERL---------ELAEQKLQQTLRKA 384
Cdd:pfam01576  154 RKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKK-EEKGRQELEKAkrklegestDLQEQIAELQAQIA 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  385 ETLPEVEAELAQRVAALSKAEE---RHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSEsnerL 461
Cdd:pfam01576  233 ELRAQLAKKEEELQAALARLEEetaQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTE----L 308

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039778538  462 QLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLV--------VTIEALKAELEQMR 514
Cdd:pfam01576  309 EDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLqemrqkhtQALEELTEQLEQAK 369
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 260-519 4.71e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.56  E-value: 4.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  260 RQAREQsqmkeRLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQ--KEDMEERITTLEKRylaaQREats 337
Cdd:COG3096    780 RAAREK-----RLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVafAPDPEAELAALRQR----RSE--- 847

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  338 vhdlndkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQT-LRKAETLPEVEAELAQRVAALSKAE---ERHGNIEE 413
Cdd:COG3096    848 -------LERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnLLADETLADRLEELREELDAAQEAQafiQQHGKALA 920

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  414 RLR--------------QMEAQLEEKNQELQRARQR-EKMNEEHNKRL----SDTVDkLLSESNErLQLHLKERMAALED 474
Cdd:COG3096    921 QLEplvavlqsdpeqfeQLQADYLQAKEQQRRLKQQiFALSEVVQRRPhfsyEDAVG-LLGENSD-LNEKLRARLEQAEE 998

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039778538  475 KNSLLRE-VENAKKQLEE---------TQHD-KDQlvvTIEALKAELEQMRLRGPS 519
Cdd:COG3096    999 ARREAREqLRQAQAQYSQynqvlaslkSSRDaKQQ---TLQELEQELEELGVQADA 1051
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
344-510 6.34e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 42.50  E-value: 6.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  344 KLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK---------AETLPEVEAELAQRVAALSKAEERHGNIEER 414
Cdd:COG1842     41 EARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlareaLERKAELEAQAEALEAQLAQLEEQVEKLKEA 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  415 LRQMEAQLEEKNQELQRARQREKMNeEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAK---KQLEE 491
Cdd:COG1842    121 LRQLESKLEELKAKKDTLKARAKAA-KAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEAAAELAAGDsldDELAE 199

                          170       180
                   ....*....|....*....|..
gi 1039778538  492 TQHDK---DQLvvtiEALKAEL 510
Cdd:COG1842    200 LEADSeveDEL----AALKAKM 217
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 162-352 7.36e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 7.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  162 KALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRS 238
Cdd:COG4942     48 KEEKALLKQLAALERRIaalARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLS 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  239 SDGSLsheDLAKVLE-LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDM 317
Cdd:COG4942    128 PEDFL---DAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL 204

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1039778538  318 EERITTLEKRYLAAQREATSVHDLNDKLENEIANK 352
Cdd:COG4942    205 EKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 343-508 7.47e-04

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 42.36  E-value: 7.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  343 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAE----------------TLPEVEAELAQRVAALSKAEE 406
Cdd:pfam04012   39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNeelarealaekkslekQAEALETQLAQQRSAVEQLRK 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  407 RHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehnkrlsdTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENA- 485
Cdd:pfam04012  119 QLAALETKIQQLKAKKNLLKARLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARADAAAELASAv 190

                          170       180
                   ....*....|....*....|....*
gi 1039778538  486 --KKQLEETQHDKDQLVVTIEALKA 508
Cdd:pfam04012  191 dlDAKLEQAGIQMEVSEDVLARLKA 215
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 154-512 7.69e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 7.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  154 VSSEVEVLKALKSLFEHHKALDEKVRErLRVALERcslLEEELGATH------------------KELMILKEQNNQKKT 215
Cdd:pfam01576  670 VSSKDDVGKNVHELERSKRALEQQVEE-MKTQLEE---LEDELQATEdaklrlevnmqalkaqfeRDLQARDEQGEEKRR 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  216 LtdgLLDGNHEQESAPSTNGKRSSDGSLSHEDLA---KVLELQEVIDRQAREQS--QMKERLASLSSHAAELEEDLDTAR 290
Cdd:pfam01576  746 Q---LVKQVRELEAELEDERKQRAQAVAAKKKLEldlKELEAQIDAANKGREEAvkQLKKLQAQMKDLQRELEEARASRD 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  291 KDLIKSEEMNTKLQREVREAMAQKEDMEerittlekrylAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERL 370
Cdd:pfam01576  823 EILAQSKESEKKLKNLEAELLQLQEDLA-----------ASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARI 891

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  371 ELAEQKLQQTLRKAETLPEVEAELAQRVAALS---KAEERHGNIEERLRQmeaQLEEKNQELQ-RARQREKMNEEHNKRL 446
Cdd:pfam01576  892 AQLEEELEEEQSNTELLNDRLRKSTLQVEQLTtelAAERSTSQKSESARQ---QLERQNKELKaKLQEMEGTVKSKFKSS 968

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039778538  447 SDTVDKLLSESNERLQLHLKERMAA---LEDKNSLLRE----VENAKKQLEETQHDKDQLVVTIEALKAELEQ 512
Cdd:pfam01576  969 IAALEAKIAQLEEQLEQESRERQAAnklVRRTEKKLKEvllqVEDERRHADQYKDQAEKGNSRMKQLKRQLEE 1041
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 246-459 9.02e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 43.38  E-value: 9.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  246 EDLAKVLElQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARK-------DLIKSEEMNT-KLQREVREAMAQKEDM 317
Cdd:PRK05771    34 EDLKEELS-NERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKvsvksleELIKDVEEELeKIEKEIKELEEEISEL 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  318 EERITTLEKRylaaQREATSVHDLNDKLENEIANKdSMHRQTEDKNRQLQERLELAEQKLQQTLRK-------------A 384
Cdd:PRK05771   113 ENEIKELEQE----IERLEPWGNFDLDLSLLLGFK-YVSVFVGTVPEDKLEELKLESDVENVEYIStdkgyvyvvvvvlK 187

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039778538  385 ETLPEVEAELAQrvAALSKAE-ERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDKLLSESNE 459
Cdd:PRK05771   188 ELSDEVEEELKK--LGFERLElEEEGTPSELIREIKEELEEIEKERESLLEElKELAKKYLEELLALYEYLEIELER 262
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 139-662 9.72e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.50  E-value: 9.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  139 LRMTVVKRQAQspagVSSEVEVLKALKSLFEHHKALDEKVRERLRVALErcslLEEELGATHKELMILKEQNNQKKTLTD 218
Cdd:TIGR00606  222 IRDQITSKEAQ----LESSREIVKSYENELDPLKNRLKEIEHNLSKIMK----LDNEIKALKSRKKQMEKDNSELELKME 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  219 GLLDGNHEQESAPSTNgkRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERL---ASLSSHAAELEEDLDTARKDLIK 295
Cdd:TIGR00606  294 KVFQGTDEQLNDLYHN--HQRTVREKERELVDCQRELEKLNKERRLLNQEKTELlveQGRLQLQADRHQEHIRARDSLIQ 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  296 SEEMNTKL---------QREVREAMA-QKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQ 365
Cdd:TIGR00606  372 SLATRLELdgfergpfsERQIKNFHTlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEK 451

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  366 LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEErHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE--HN 443
Cdd:TIGR00606  452 KQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQlnHH 530

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  444 KRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENaKKQLEETQHDK-DQLVVTIEALK------AELEQMRlr 516
Cdd:TIGR00606  531 TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPN-KKQLEDWLHSKsKEINQTRDRLAklnkelASLEQNK-- 607

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  517 gpslHHGRPHLGSVPDFRFSVADGHVDAYSTsavlrrpqkgrlaalRDEPSKVQTLNEQDWERAQQASVLANVAQAFESD 596
Cdd:TIGR00606  608 ----NHINNELESKEEQLSSYEDKLFDVCGS---------------QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQF 668

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039778538  597 VDVSDGEDDRdtllssvdlLSPSGQADAQTLAmMLQEQLDAINKEIRLIQEEKENTEQRAEEIESR 662
Cdd:TIGR00606  669 ITQLTDENQS---------CCPVCQRVFQTEA-ELQEFISDLQSKLRLAPDKLKSTESELKKKEKR 724
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 357-513 1.12e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.40  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  357 RQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALskaEERHGNIEERLRQMEAQLEEKNQELQRARQRE 436
Cdd:COG3096    525 EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARIKELAARA 601

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039778538  437 KMNEEHNKRLsdtvdkllsesnERLQLHLKErmaALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQM 513
Cdd:COG3096    602 PAWLAAQDAL------------ERLREQSGE---ALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 113-524 1.15e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.24  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  113 ELKAERNNTRLLLEH-LECLVSRHERSLRmTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKvrERLRVALERCSL 191
Cdd:pfam01576  320 ELRSKREQEVTELKKaLEEETRSHEAQLQ-EMRQKHTQALEELTEQLEQAKRNKANLEKAKQALES--ENAELQAELRTL 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  192 LEEELGATHK---------ELMI-LKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKV-LELQeviDR 260
Cdd:pfam01576  397 QQAKQDSEHKrkklegqlqELQArLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLeSQLQ---DT 473

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  261 QAREQSQMKERLaSLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQ----KEDMEERITTLEKRYLAAQREAT 336
Cdd:pfam01576  474 QELLQEETRQKL-NLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQlsdmKKKLEEDAGTLEALEEGKKRLQR 552

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  337 SVHDLNDKLENEIANKDSMHRQTE-------------DKNRQLQERLELAEQKLQQTL--------RKAETLPEVEAELA 395
Cdd:pfam01576  553 ELEALTQQLEEKAAAYDKLEKTKNrlqqelddllvdlDHQRQLVSNLEKKQKKFDQMLaeekaisaRYAEERDRAEAEAR 632

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  396 QRVA-------ALSKAEERHGNIEERLRQMEAQLEE---------KN-QELQRA-RQREKMNEEHNKRLSDTVDKLLSES 457
Cdd:pfam01576  633 EKETralslarALEEALEAKEELERTNKQLRAEMEDlvsskddvgKNvHELERSkRALEQQVEEMKTQLEELEDELQATE 712

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  458 NERLQLHLKerMAAL----------------EDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLH 521
Cdd:pfam01576  713 DAKLRLEVN--MQALkaqferdlqardeqgeEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAAN 790


                   ...
gi 1039778538  522 HGR 524
Cdd:pfam01576  791 KGR 793
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 31-473 1.18e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   31 DADSHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQ---LNTALPQEFAAL---TKELNVCREQL 104
Cdd:pfam15921  321 DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLhkrEKELSLEKEQN 400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  105 LE-------REEEIAELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEK 177
Cdd:pfam15921  401 KRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  178 VRERL---RVALER---------CSLLEEE--LGATHKELMILKEQNNQK-KTLTDGLLDGNHEQESAPSTNGKRssdgs 242
Cdd:pfam15921  480 VVEELtakKMTLESsertvsdltASLQEKEraIEATNAEITKLRSRVDLKlQELQHLKNEGDHLRNVQTECEALK----- 554

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  243 LSHEDLAKVLE-LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEeri 321
Cdd:pfam15921  555 LQMAEKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE--- 631

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  322 ttLEKRYL--AAQREATSVHDLN---DKLENEIAN-KDSMHRQTEDKN------RQLQERLELAEQKLQQTLRKAET--- 386
Cdd:pfam15921  632 --LEKVKLvnAGSERLRAVKDIKqerDQLLNEVKTsRNELNSLSEDYEvlkrnfRNKSEEMETTTNKLKMQLKSAQSele 709

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  387 ---------------------------------------------------------LPEVEAELAQRVAALSKAEERHG 409
Cdd:pfam15921  710 qtrntlksmegsdghamkvamgmqkqitakrgqidalqskiqfleeamtnankekhfLKEEKNKLSQELSTVATEKNKMA 789

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039778538  410 NIEERLRQMEAQLEEKNQELQRARQREKMneehnkRLSDTVDKLLSESNERLQLHLKERMAALE 473
Cdd:pfam15921  790 GELEVLRSQERRLKEKVANMEVALDKASL------QFAECQDIIQRQEQESVRLKLQHTLDVKE 847
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
253-521 1.22e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQ 332
Cdd:COG4372     70 QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  333 REATSVHDLNDKLENEIAN--KDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS--KAEERH 408
Cdd:COG4372    150 EELKELEEQLESLQEELAAleQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLeaKDSLEA 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  409 GNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQ 488
Cdd:COG4372    230 KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1039778538  489 LEETQHDKDQLVVTIEALKAELEQMRLRGPSLH 521
Cdd:COG4372    310 IGALEDALLAALLELAKKLELALAILLAELADL 342
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 323-444 1.42e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153364 [Multi-domain]  Cd Length: 258  Bit Score: 41.96  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  323 TLEKRYLAAQREATSVHDLNDKLENEIAN----------KDSMHRQTE---DKNRQLQERLELAEQKLQQTLRKAETLPE 389
Cdd:cd07680     61 SLERAWGAIMTEADKVSELHQEVKNNLLNedlekvknwqKDAYHKQIMggfKETKEAEDGFRKAQKPWAKKMKELEAAKK 140

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039778538  390 V------EAELAQRVAALSKAEErhGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNK 444
Cdd:cd07680    141 AyhlackEEKLAMTREANSKAEQ--SVTPEQQKKLQDKVDKCKQDVQKTQEKyEKVLDDVGK 200
mukB PRK04863
chromosome partition protein MukB;
112-487 1.52e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  112 AELKAERNNTRLLLEHLECLVSRH---------ERSLRMTVVKRQaqspagvssevEVLKALKSLFEHHKaldeKVRERL 182
Cdd:PRK04863   803 ATLSFDVQKLQRLHQAFSRFIGSHlavafeadpEAELRQLNRRRV-----------ELERALADHESQEQ----QQRSQL 867

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  183 RVALERCSLLEEELGathkELMILKEQnnqkkTLTDglldgnhEQESApstngkrssdgslsHEDLAKVLELQEVIDRQA 262
Cdd:PRK04863   868 EQAKEGLSALNRLLP----RLNLLADE-----TLAD-------RVEEI--------------REQLDEAEEAKRFVQQHG 917

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  263 REQSQMKERLASLSSHAAELEEdldtarkdlikseemntkLQREVREAMAQKEDMEERITTLEkrYLAAQREATSVHDLN 342
Cdd:PRK04863   918 NALAQLEPIVSVLQSDPEQFEQ------------------LKQDYQQAQQTQRDAKQQAFALT--EVVQRRAHFSYEDAA 977

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  343 DKLEneiankdsmhrQTEDKNRQLQERLELAEqklQQTLRKAETLPEVEAELAQRVAALSKAEERHgnieERLRQMEAQL 422
Cdd:PRK04863   978 EMLA-----------KNSDLNEKLRQRLEQAE---QERTRAREQLRQAQAQLAQYNQVLASLKSSY----DAKRQMLQEL 1039

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  423 EEKNQEL---------QRARQREkmnEEHNKRLSDT------VDKLLSESNERLQlHLKERMAALEDKNSLLRE-VENAK 486
Cdd:PRK04863  1040 KQELQDLgvpadsgaeERARARR---DELHARLSANrsrrnqLEKQLTFCEAEMD-NLTKKLRKLERDYHEMREqVVNAK 1115


                   .
gi 1039778538  487 K 487
Cdd:PRK04863  1116 A 1116
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 876-938 1.60e-03

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 38.02  E-value: 1.60e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039778538  876 QWDGPTVVVWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQ 938
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQ 61
mukB PRK04863
chromosome partition protein MukB;
325-517 1.63e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  325 EKRYLAAQREAtsvhdlndkLENEIANKDSMHRQTEDKNRQLQErlelAEQKLQQTLRKAETLPEVEAELAQRVAALSKA 404
Cdd:PRK04863   507 EQRHLAEQLQQ---------LRMRLSELEQRLRQQQRAERLLAE----FCKRLGKNLDDEDELEQLQEELEARLESLSES 573

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  405 EERHGNIEERLRQMEAQLEEKNQELQRARQrekmnEEHNkrlsdtvdklLSESNERLQLHLKErmaALEDKNSLLREVEN 484
Cdd:PRK04863   574 VSEARERRMALRQQLEQLQARIQRLAARAP-----AWLA----------AQDALARLREQSGE---EFEDSQDVTEYMQQ 635

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1039778538  485 AKKQLEETQHDKDQLVVTIEALKAELEQMRLRG 517
Cdd:PRK04863   636 LLERERELTVERDELAARKQALDEEIERLSQPG 668
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 174-512 1.68e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 42.64  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  174 LDEKVRERL---RVALERCSLLEEELgaTHKELMILKEqnNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDL-- 248
Cdd:COG5185    143 LDEIADIEAsygEVETGIIKDIFGKL--TQELNQNLKK--LEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGse 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  249 ------AKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTAR-KDLIKSEEMNTKLQREVREAMAQKEDMEERI 321
Cdd:COG5185    219 stllekAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRlEKLGENAESSKRLNENANNLIKQFENTKEKI 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  322 TTLEKrylaaqreatsvhdlndkleneianKDSMHRQTEDKNRQLQERLElaEQKLQQTLRKAET-LPEVEAELAQRVAA 400
Cdd:COG5185    299 AEYTK-------------------------SIDIKKATESLEEQLAAAEA--EQELEESKRETETgIQNLTAEIEQGQES 351

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  401 LSKAEERHGN-------------IEERLRQMEAQLEEKNQELQRARQ-REKMNEEHNKRLSDTVdKLLSESNERLQlhlk 466
Cdd:COG5185    352 LTENLEAIKEeienivgevelskSSEELDSFKDTIESTKESLDEIPQnQRGYAQEILATLEDTL-KAADRQIEELQ---- 426

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1039778538  467 ermAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQ 512
Cdd:COG5185    427 ---RQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAY 469
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 999-1046 1.76e-03

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 38.05  E-value: 1.76e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1039778538  999 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSF 1046
Cdd:cd09501     11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRF 58
PRK12704 PRK12704
phosphodiesterase; Provisional
 364-514 1.77e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  364 RQLQERLELAEQKLQQTLRKAETlpevEAELAQRVAALSKAEERHgnieERLRQMEAQLEEKNQELQRARQREKMNEEHn 443
Cdd:PRK12704    27 KIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALLEAKEEIH----KLRNEFEKELRERRNELQKLEKRLLQKEEN- 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039778538  444 krlsdtvdkllsesnerlqlhLKERMAALEDKNsllREVENAKKQLEETQHDkdqlvvtIEALKAELEQMR 514
Cdd:PRK12704    98 ---------------------LDRKLELLEKRE---EELEKKEKELEQKQQE-------LEKKEEELEELI 137
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 1075-1141 1.78e-03

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 38.02  E-value: 1.78e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039778538 1075 RDVLVWSNDRVIRWILSIGLKEYANNLIESGVHG-ALLALDETfDFSALALllqiptQNTQARAVLER 1141
Cdd:cd09512      2 RPVSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS-KLKALGI------TSSSDRSLLKK 62
46 PHA02562
endonuclease subunit; Provisional
 207-430 1.96e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.31  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  207 KEQNNQKKTLtDGLLDGNHEQESAPSTNGKRSSdgSLSHEDLAkvlELQEVIDRQAREQSQMKERLASLSSHAAELEEDL 286
Cdd:PHA02562   177 RELNQQIQTL-DMKIDHIQQQIKTYNKNIEEQR--KKNGENIA---RKQNKYDELVEEAKTIKAEIEELTDELLNLVMDI 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  287 DTARKDLIKSEEMNTKLQREV----REA------------MAQKEDMEERITTLEKRYLAAQreaTSVHDLNDKLENEIA 350
Cdd:PHA02562   251 EDPSAALNKLNTAAAKIKSKIeqfqKVIkmyekggvcptcTQQISEGPDRITKIKDKLKELQ---HSLEKLDTAIDELEE 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  351 NKDSMHRQTEdKNRQLQERLELAEQKLQQTLRKAEtlpEVEAElaqrvaaLSKAEERHGNIEERLRQMEAQLEEKNQELQ 430
Cdd:PHA02562   328 IMDEFNEQSK-KLLELKNKISTNKQSLITLVDKAK---KVKAA-------IEELQAEFVDNAEELAKLQDELDKIVKTKS 396
PLN02939 PLN02939
transferase, transferring glycosyl groups
 179-518 2.25e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 42.20  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  179 RERLRVAlerCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQE-------SAPSTNGKRSSDGSLSHEDLAKV 251
Cdd:PLN02939    28 RRRLAVS---CRARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQlentslrTVMELPQKSTSSDDDHNRASMQR 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  252 LELQEVIDRQAREQSQMKERLASLssHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY--- 328
Cdd:PLN02939   105 DEAIAAIDNEQQTNSKDGEQLSDF--QLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLset 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  329 -----LAAQrEATSVHDLNDKLENeiANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK--AETLPEVEAELAQRVAAL 401
Cdd:PLN02939   183 darikLAAQ-EKIHVEILEEQLEK--LRNELLIRGATEGLCVHSLSKELDVLKEENMLLKddIQFLKAELIEVAETEERV 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  402 SKAEERHGNIEERLRQMEAQLE------------------EKNQELQRARQREKMNEEH-------NKRLSDTVDKL--- 453
Cdd:PLN02939   260 FKLEKERSLLDASLRELESKFIvaqedvsklsplqydcwwEKVENLQDLLDRATNQVEKaalvldqNQDLRDKVDKLeas 339

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039778538  454 LSESN------ERLQLhLKERMAALEDKnsLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGP 518
Cdd:PLN02939   340 LKEANvskfssYKVEL-LQQKLKLLEER--LQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEHP 407
Caldesmon pfam02029
Caldesmon;
174-470 2.29e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.16  E-value: 2.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  174 LDEKVRERLRVALERCSLLEEELGATHKELMILKEQNN-------QKKTLTDGLLDGNHEQESapSTNGKRSSDGSLSHE 246
Cdd:pfam02029   71 REERRQKRLQEALERQKEFDPTIADEKESVAERKENNEeeensswEKEEKRDSRLGRYKEEET--EIREKEYQENKWSTE 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  247 DLAKVLELQEVIDRQAREQSQMKERlaslssHAAElEEDLDTARKDLIKSEEMNTKLQREVR---EAMAQKEDMEERITT 323
Cdd:pfam02029  149 VRQAEEEGEEEEDKSEEAEEVPTEN------FAKE-EVKDEKIKKEKKVKYESKVFLDQKRGhpeVKSQNGEEEVTKLKV 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  324 LEKRYLAAQREAtsvhdlnDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpeVEAELAQRvaalsK 403
Cdd:pfam02029  222 TTKRRQGGLSQS-------QEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAE----LELEELKK-----K 285

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039778538  404 AEERHGNIEERLRQMEAqlEEKnqelqrarQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMA 470
Cdd:pfam02029  286 REERRKLLEEEEQRRKQ--EEA--------ERKLREEEEKRRMKEEIERRRAEAAEKRQKLPEDSSS 342
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 246-491 2.32e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  246 EDLAKVLELQEVIDRQAREQSQMKERLAslsshAAELEEDLDTARKDLIKSEEMNtKLQREVREAMAQKEDMEERITTLE 325
Cdd:pfam13868  120 EKLEKQRQLREEIDEFNEEQAEWKELEK-----EEEREEDERILEYLKEKAEREE-EREAEREEIEEEKEREIARLRAQQ 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  326 KRYLAAQREATsvhDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETlpeveaelaqrvaalsKAE 405
Cdd:pfam13868  194 EKAQDEKAERD---ELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERR----------------LAE 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  406 ERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdkllsesNERLQLHLKERMAALEDKNSLLREVENA 485
Cdd:pfam13868  255 EAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQI-------EEREEQRAAEREEELEEGERLREEEAER 327


                   ....*.
gi 1039778538  486 KKQLEE 491
Cdd:pfam13868  328 RERIEE 333
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 45-276 2.87e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  125 LEHLECLVSRHERSLRMTVVKRQAQ---SPAGVSSEVEVLKALKSLFEHhkalDEKVRERLRVALERCSLLEEELGATHK 201
Cdd:COG4942     99 LEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPA----RREQAEELRADLAELAALRAELEAERA 174

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039778538  202 ELM-ILKEQNNQKKTLTDGLLDgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLS 276
Cdd:COG4942    175 ELEaLLAELEEERAALEALKAE---RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
PRK12705 PRK12705
hypothetical protein; Provisional
 364-515 3.58e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 41.23  E-value: 3.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  364 RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERlrqmeaqlEEKNQELQRARQREKMNEEHN 443
Cdd:PRK12705    26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  444 KRLSDTVDKLLSESNerlqlHLKERMAALEDKNSLLREV---------ENAKKQL-----EETQHDKDQLVVTIEAlKAE 509
Cdd:PRK12705    98 EKLDNLENQLEEREK-----ALSARELELEELEKQLDNElyrvagltpEQARKLLlklldAELEEEKAQRVKKIEE-EAD 171


                   ....*.
gi 1039778538  510 LEQMRL 515
Cdd:PRK12705   172 LEAERK 177
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 284-512 3.75e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 3.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  284 EDLDTARKDLIKSEEMN----TKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQT 359
Cdd:TIGR04523   78 KILEQQIKDLNDKLKKNkdkiNKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKL 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  360 EDKNRQLQERLELAEQKL----QQTLRKAETLPEVEAELAQRVAALSKAEERhgniEERLRQMEAQLEE-KNQELQRARQ 434
Cdd:TIGR04523  158 NNKYNDLKKQKEELENELnlleKEKLNIQKNIDKIKNKLLKLELLLSNLKKK----IQKNKSLESQISElKKQNNQLKDN 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  435 REKMNEEHNKR---LSDTVDKLLSESNErlQLHLKERmaaLEDKNSllrEVENAKKQLEETQHDKDQLVVTIEALKAELE 511
Cdd:TIGR04523  234 IEKKQQEINEKtteISNTQTQLNQLKDE--QNKIKKQ---LSEKQK---ELEQNNKKIKELEKQLNQLKSEISDLNNQKE 305


                   .
gi 1039778538  512 Q 512
Cdd:TIGR04523  306 Q 306
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 246-446 3.88e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  246 EDLAKVLELQEVIDRQAREQSQMKER--LASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITT 323
Cdd:pfam13868  130 EEIDEFNEEQAEWKELEKEEEREEDEriLEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAK 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  324 LEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSK 403
Cdd:pfam13868  210 LYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL 289

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039778538  404 A---------EERHgniEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRL 446
Cdd:pfam13868  290 EhrrelekqiEERE---EQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
PRK09039 PRK09039
peptidoglycan -binding protein;
255-433 5.11e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.72  E-value: 5.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  255 QEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRyLAAQRe 334
Cdd:PRK09039    52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQE-LDSEK- 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  335 ATSVHDLndkleneiankdsmhRQTEDKNRQLQErlelaeqklqqtLRkaetlpeveAELAQRVAALSKAEERHGNIEER 414
Cdd:PRK09039   130 QVSARAL---------------AQVELLNQQIAA------------LR---------RQLAALEAALDASEKRDRESQAK 173

                          170       180
                   ....*....|....*....|...
gi 1039778538  415 L----RQMEAQLEEKNQELQRAR 433
Cdd:PRK09039   174 IadlgRRLNVALAQRVQELNRYR 196
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 271-514 5.34e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 40.99  E-value: 5.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  271 RLASLSSHAAELEEDLD------------TARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY------LAAQ 332
Cdd:pfam06160   61 SLPDIEELLFEAEELNDkyrfkkakkaldEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYrelrktLLAN 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  333 REA--TSVHDLNDKLEN--------EIANKDSMHRQTEDKNRQLQERLELAEQKLQQT---LRKAET-LPEVEAELAQRV 398
Cdd:pfam06160  141 RFSygPAIDELEKQLAEieeefsqfEELTESGDYLEAREVLEKLEEETDALEELMEDIpplYEELKTeLPDQLEELKEGY 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  399 AALSKAEER--HGNIEERLRQMEAQLEE-----KNQELQRArqrEKMNEEHNKRLSDTVDKLLSESNERLQLHlkERMAA 471
Cdd:pfam06160  221 REMEEEGYAleHLNVDKEIQQLEEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVE--KNLPE 295

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039778538  472 LEDknsllrEVENAKKQLEETQHDKDQL----------VVTIEALKAELEQMR 514
Cdd:pfam06160  296 IED------YLEHAEEQNKELKEELERVqqsytlneneLERVRGLEKQLEELE 342
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 389-660 5.35e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 5.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  389 EVEAELAQRVAALSKAEERhgniEERLRQMeaqLEEKNQELQR-ARQREKMNEehnkrlsdtVDKLLSESNE-RLQLHLK 466
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEEN----IERLDLI---IDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLK 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  467 ERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRphlgsVPDFRFSVADGHVD--- 543
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE-----QLRVKEKIGELEAEias 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  544 AYSTSAVLRRPQK---GRLAALRDEPSKVQ-TLNEQDWERAQQASVLANVAQAFESDvdvsdgEDDRDTLLSSVDLLSPS 619
Cdd:TIGR02169  306 LERSIAEKERELEdaeERLAKLEAEIDKLLaEIEELEREIEEERKRRDKLTEEYAEL------KEELEDLRAELEEVDKE 379

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1039778538  620 GQA------DAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIE 660
Cdd:TIGR02169  380 FAEtrdelkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 320-516 6.09e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.65  E-value: 6.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  320 RITTLEKRYLAAQREATSVHDL----NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPE------ 389
Cdd:pfam07888   28 RAELLQNRLEECLQERAELLQAqeaaNRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEkykels 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  390 -VEAELAQRVAALSKAEERHG----NIEERLRQMEAQLEEKNQELQRARQREKM------NEEHNKRLSDTVDKLLSESN 458
Cdd:pfam07888  108 aSSEELSEEKDALLAQRAAHEarirELEEDIKTLTQRVLERETELERMKERAKKagaqrkEEEAERKQLQAKLQQTEEEL 187

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039778538  459 ERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:pfam07888  188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQER 245
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 249-513 6.17e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.88  E-value: 6.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  249 AKVLELQEVIDRQAREQSQM----KERLASLSSHAAELEEDLDTARKdliKSEEMNTKLQ----REVREAMAQKEDMEEr 320
Cdd:pfam05557    2 AELIESKARLSQLQNEKKQMelehKRARIELEKKASALKRQLDRESD---RNQELQKRIRllekREAEAEEALREQAEL- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  321 iTTLEKRYLAAQREA--------TSVHDLNDKLENEIA-------NKDSMHRQTEDKNRQLQERLEL-------AEQKLQ 378
Cdd:pfam05557   78 -NRLKKKYLEALNKKlnekesqlADAREVISCLKNELSelrrqiqRAELELQSTNSELEELQERLDLlkakaseAEQLRQ 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  379 QTLRKAETLPEVEA---ELAQRVAALSKAEERHGNIEERLrqmeAQLEEKNQELQRARqrekmneEHNKRLSDTVDK--L 453
Cdd:pfam05557  157 NLEKQQSSLAEAEQrikELEFEIQSQEQDSEIVKNSKSEL----ARIPELEKELERLR-------EHNKHLNENIENklL 225

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039778538  454 LSESNERLQLHL------KERMAALEDKNS-LLREVENAKKQLEETQHDkdqlVVTIEALKAELEQM 513
Cdd:pfam05557  226 LKEEVEDLKRKLereekyREEAATLELEKEkLEQELQSWVKLAQDTGLN----LRSPEDLSRRIEQL 288
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
 260-491 6.73e-03

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.


Pssm-ID: 464481  Cd Length: 528  Bit Score: 40.59  E-value: 6.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  260 RQAREQSQMKERLASLSShaaeLEEDLdtARKDLIKseemntKLQREVREAMAQKEDMEERITTLEKRYLAAQREATS-- 337
Cdd:pfam15066  292 QENCKTPDTEQSFESLQP----LEEDM--ALNEVLQ------KLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKqq 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  338 -----VHDLNDKLENEIANKDSMHRQTEDKNRQLQ---ERLELAEQKLQQTLRKAETLpevEAELAQRVAALSKAEERHG 409
Cdd:pfam15066  360 vfvdiINKLKENVEELIEDKYNVILEKNDINKTLQnlqEILANTQKHLQESRKEKETL---QLELKKIKVNYVHLQERYI 436

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  410 N-IEERLR------QMEAQLEEKNQELQRARQrekMNEEHNKRLSDTVDKLLSESNERLQ--LHLKERMAALEDKNslLR 480
Cdd:pfam15066  437 TeMQQKNKsvsqclEMDKTLSKKEEEVERLQQ---LKGELEKATTSALDLLKREKETREQefLSLQEEFQKHEKEN--LE 511

                          250
                   ....*....|.
gi 1039778538  481 EVENAKKQLEE 491
Cdd:pfam15066  512 ERQKLKSRLEK 522
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
280-396 8.29e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.04  E-value: 8.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  280 AELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQ---REATSVHDLNDklENEIANKDSMH 356
Cdd:COG1842     94 AELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKaqeKVNEALSGIDS--DDATSALERME 171

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1039778538  357 RQTEDKNRQLQERLELAEQK-LQQTLRKAETLPEVEAELAQ 396
Cdd:COG1842    172 EKIEEMEARAEAAAELAAGDsLDDELAELEADSEVEDELAA 212
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
296-511 8.44e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 8.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  296 SEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQ 375
Cdd:COG4372      1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  376 KLQQTlrkaetlpevEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTV---DK 452
Cdd:COG4372     81 ELEEL----------NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIaerEE 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039778538  453 LLSESNERLQlHLKERMAALEDKNSLLrEVENAKKQLEETQHDKDQLVVTIEALKAELE 511
Cdd:COG4372    151 ELKELEEQLE-SLQEELAALEQELQAL-SEAEAEQALDELLKEANRNAEKEEELAEAEK 207
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 44-403 8.45e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 8.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538   44 LEERDRLLDTLRETQETLaltQGKLHEVGHERDSLQRQLNT------ALPQEFAALTKELNVCREQLLEREEEIAELKAE 117
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRI---ENRLDELSQELSDASRKIGEiekeieQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  118 rnntrllLEHLECLVSRHERSLrmtvvkrqaqspAGVSSEVEVLKA--LKSLFEHHKALDEKVRERLRVALERCSLLEEE 195
Cdd:TIGR02169  760 -------LKELEARIEELEEDL------------HKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  196 LGATHKELMILKEQNNQKKTLTDGLLDgnheqesapstngKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASL 275
Cdd:TIGR02169  821 LNRLTLEKEYLEKEIQELQEQRIDLKE-------------QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778538  276 SSHAAELEEDLDTARKdliKSEEMNTKLQRE---VREAMAQKEDMEERITTLEKRYLAAQREATSVHDLnDKLENEIANK 352
Cdd:TIGR02169  888 KKERDELEAQLRELER---KIEELEAQIEKKrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRV 963

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039778538  353 DSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSK 403
Cdd:TIGR02169  964 EEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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